Journal articles on the topic 'Histidine'
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Nair, C. P. P., and E. L. Robert Stokstad. "Effect of Hormones and Protein Level on Induction of Enzymes Involved in Histidine Degradation and Folate Metabolism." Pteridines 2, no. 3 (September 1990): 183–87. http://dx.doi.org/10.1515/pteridines.1990.2.3.183.
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Summary The effects of the hormones thyroxine, glucagon and hydrocortisone, and of protein level on hepatic histidase, urocanase, and certain folate enzymes were studied in rats. Hypothyroidism, induced either by feeding thiouracil or by thyroidectomy, increased histidase, urocanase, and the folate dependent enzyme formiminotransferase, and increased histidine metabolism as measured by oxidation of the 2-ring carbon of histidine to carbon dioxide. Hyperthyroidism, produced by feeding thyroid powder, decreased histidine oxidation and liver levels of this enzyme. Glucagon and hydrocortisone increased histidine oxidation and increased levels of histidase, urocanase and formiminotransferase. Elevated levels of casein and soy protein produced four to eight fold increases in histidase and urocanase, and 50% increases in formiminotransferase. Thus, increases in histidase and urocanase involved in the formation of formiminoglutamic acid (FIGlu) were accompanied by increases in the FIGlu metabolizing enzyme formiminotransferase.
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Akirthasary, Desty. "REVIEW ARTIKEL : ENZIM L-HISTIDIN DEKARBOKSILASE DAN MEKANISME PENGHAMBATAN." Unesa Journal of Chemistry 10, no. 2 (May 30, 2021): 147–57. http://dx.doi.org/10.26740/ujc.v10n2.p147-157.
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Abstrak. Enzim L-Histidin dekarboksilase merupakan suatu enzim yang digunakan untuk mengkatalis histidin dalam membentuk histamin. Enzim L-Histidin dekarboksilase dapat dimanfaatkan sebagai antialergi, antihistamin serta menjadi komponen dalam memahami mekanisme histamin. Enzim L-histidin dekarboksilase dapat diperoleh dari asam amino yang ada didalam daging, keju dan ikan. Namun sumber utama yaitu ikan busuk disebabkan aktivitas mikroba diatas 4oC dengan waktu cukup lama, kemudian enzim L-Histidin dekarboksilase yang ada dalam ikan akan disintesis menghasilkan histamin. Enzim L-Histidin dekarboksilase terdapat dalam bakteri mesofilik yang tumbuh pada suhu 30oC-37oC. Bakteri tersebut antara lain Morganella morganii, Klebsiella pneumonia, Hafnia alvei, Citrobacter freundii, Clostridium perfringens, Enterobacter aerogenes, Vibrio alginolyticus, dan Proteus sp yang dapat memberikan pengaruh negatif terhadap kesehatan antara lain diare akibat keracunan, sakit kepala, hipotensi, pruritus dan tubuh akan terlihat memerah. Sehingga diperlukan adanya penghambatan aktivitas enzim L- Histidin dekarboksilase. Penghambatan dapat dilakukan untuk mengontrol terbentuknya histamin dengan cara penambahan senyawa yang akan merusak dinding sel suatu bakteri yang mengakibatkan terhentinya fungsi kerja enzim tersebut. Senyawa penghambat yang dapat digunakan dapat berupa senyawa kimiawi seperti asam benzoat atau dapat juga menggunakan senyawa alami yang memiliki kandungan flavonoid, saponin, terpenoid, dan tanin yang akan mencegah pertumbuhan bakteri. Senyawa penghambat tersebut banyak ditemukan pada Teh Hijau, asam jawa, bawang merah atau tanaman rempah lainnya.
Kata Kunci : Enzim L-Histidin dekarboksilase, Histidin, Histamin,
Abstract. The enzyme L-Histidine decarboxylase is an enzyme used to catalyze histidine to form histamine. The enzyme L-Histidine decarboxylase can be used as antiallergy, antihistamine and a component in understanding the mechanism of histamine. The enzyme L-histidine decarboxylase can be obtained from amino acids present in meat, cheese and fish. However, the main source is rotten fish due to microbial activity above 4oC for a long time, then the L-Histidine decarboxylase enzyme in fish will be synthesized to produce histamine. L-Histidine decarboxylase enzyme is present in mesophilic bacteria that grow at temperatures of 30oC-37oC. These bacteria include Morganella morganii, Klebsiella pneumonia, Hafnia alvei, Citrobacter freundii, Clostridium perfringens, Enterobacter aerogenes, Vibrio alginolyticus, and Proteus sp which can have negative effects on health, including diarrhea due to poisoning, headaches, hypotension, pruritus and the body. looks red. So that it is necessary to inhibit the activity of the enzyme L-Histidine decarboxylase. Inhibition can be done to control the formation of histamine by adding compounds that will damage the cell wall of a bacteria which results in the cessation of the enzyme function. Inhibition compounds that can be used can be chemical compounds such as benzoic acid or you can also use natural compounds that contain flavonoids, saponins, terpenoids, and tannins that will prevent bacterial growth. These inhibiting compounds are found in green tea, tamarind, onions or other spices.
Keyword : Decarboxylated L-Histidine Enxymes, HIstidin, Histamine.
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Borisova-, Galina, and Olga Bessonova-. "HISTIDINE BIOTRANSFORMATION MEDIATED BY L-HISTIDINE-AMMONIA-LYASE." Foods and Raw Materials 1, no. 2 (December 20, 2013): 37–41. http://dx.doi.org/10.12737/2052.
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He, Jiaxi, Songhui Xu, and A. James Mixson. "The Multifaceted Histidine-Based Carriers for Nucleic Acid Delivery: Advances and Challenges." Pharmaceutics 12, no. 8 (August 14, 2020): 774. http://dx.doi.org/10.3390/pharmaceutics12080774.
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Histidines incorporated into carriers of nucleic acids may enhance the extracellular stability of the nanoparticle, yet aid in the intracellular disruption of the nanoparticle, enabling the release of the nucleic acid. Moreover, protonation of histidines in the endosomes may result in endosomal swelling with subsequent lysis. These properties of histidine are based on its five-member imidazole ring in which the two nitrogen atoms may form hydrogen bonds or act as a base in acidic environments. A wide variety of carriers have integrated histidines or histidine-rich domains, which include peptides, polyethylenimine, polysaccharides, platform delivery systems, viral phages, mesoporous silica particles, and liposomes. Histidine-rich carriers have played key roles in our understanding of the stability of nanocarriers and the escape of the nucleic acids from endosomes. These carriers show great promise and offer marked potential in delivering plasmids, siRNA, and mRNA to their intracellular targets.
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Yang, S. H., C. H. Wu, and W. Y. Lin. "Chemical modification of aminopeptidase isolated from Pronase." Biochemical Journal 302, no. 2 (September 1, 1994): 595–600. http://dx.doi.org/10.1042/bj3020595.
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Chemical modification of aminopeptidase from pronase has revealed two important histidines in enzyme catalysis. In the absence of metal ions, modification of the readily-modified histidine (pKa 6.9 +/- 0.5) results in a drastic loss of activity, indicating that this residue is indispensible for enzyme activity. In the presence of CaCl2, the modified enzyme still retains approx. 60% of the activity, whereas modification of another histidine (pKa 7.7 +/- 0.2) leads to a dramatic loss of activity. In fact, the enzyme with the first histidine being modified is active only in the presence of metal ions. Moreover, modification of the second histidine is prevented by the presence of Ca(II). These results indicate that the second histidine is serving as a ligand for Ca(II) and the bound Ca(II) is directly involved in enzyme catalysis. The c.d. spectra of the modified and unmodified enzymes in the absence or presence of CaCl2 are all very similar, indicating that no gross conformational changes in protein occur upon modification or by the presence of Ca(II). Modification of both histidines is prevented by the presence of a competitive inhibitor, suggesting that they are located in the active centre. Modification of 11 amino groups, two tyrosines, or four arginines causes no appreciable inactivation of the enzyme, indicating that these residues are not directly involved in enzyme catalysis.
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Brosnan, Margaret E., and John T. Brosnan. "Histidine Metabolism and Function." Journal of Nutrition 150, Supplement_1 (October 1, 2020): 2570S—2575S. http://dx.doi.org/10.1093/jn/nxaa079.
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ABSTRACT Histidine is a dietary essential amino acid because it cannot be synthesized in humans. The WHO/FAO requirement for adults for histidine is 10 mg · kg body weight−1 · d−1. Histidine is required for synthesis of proteins. It plays particularly important roles in the active site of enzymes, such as serine proteases (e.g., trypsin) where it is a member of the catalytic triad. Excess histidine may be converted to trans-urocanate by histidine ammonia lyase (histidase) in liver and skin. UV light in skin converts the trans form to cis-urocanate which plays an important protective role in skin. Liver is capable of complete catabolism of histidine by a pathway which requires folic acid for the last step, in which glutamate formiminotransferase converts the intermediate N-formiminoglutamate to glutamate, 5,10 methenyl-tetrahydrofolate, and ammonia. Inborn errors have been recognized in all of the catabolic enzymes of histidine. Histidine is required as a precursor of carnosine in human muscle and parts of the brain where carnosine appears to play an important role as a buffer and antioxidant. It is synthesized in the tissue by carnosine synthase from histidine and β-alanine, at the expense of ATP hydrolysis. Histidine can be decarboxylated to histamine by histidine decarboxylase. This reaction occurs in the enterochromaffin-like cells of the stomach, in the mast cells of the immune system, and in various regions of the brain where histamine may serve as a neurotransmitter.
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Van Dam, ME, GE Wuenschell, and FH Arnold. "Metal affinity precipitation of proteins." Biotechnology and Applied Biochemistry 11, no. 5 (October 1989): 492–502. http://dx.doi.org/10.1111/j.1470-8744.1989.tb00071.x.
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Proteins containing multiple surface‐accessible histidine residues can be precipitated using small quantities of bis‐copper chelates. The chelates serve to crosslink the proteins, presumably via the accessible histidines, leading to the formation of large, insoluble complexes. When excess copper chelate is used to carry out the precipitation, the resulting precipitate has a stoichiometry of 1:1 copper:accessible histidine. The precipitation is analogous to antibody‐antigen precipitin reactions and can be described qualitatively using simple equilibrium theory developed for those systems. Human hemoglobin contains a large number of surface histidines and is efficiently precipitated by the copper salt CuSO4 as well as by bis‐copper chelates. Sperm whale myoglobin contains many fewer surface histidines and is precipitated only by the bis‐chelates. The effects of the number of accessible histidines on the protein, the chain length separating the two chelates, and the pH on the precipitation reaction have been investigated.
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Muller, Ludovic, Shelley N. Jackson, and Amina S. Woods. "Histidine, the less interactive cousin of arginine." European Journal of Mass Spectrometry 25, no. 2 (April 2019): 212–18. http://dx.doi.org/10.1177/1469066718791793.
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Electrostatic interactions are one of the main factors influencing biomolecular conformation. The formation of noncovalent complexes by electrostatic interactions is governed by certain amino acid residues and post-translational modifications. It has been demonstrated that adjacent arginine forms noncovalent complex with phosphate; however, histidine noncovalent complexes have rarely been investigated. In the present work, we compare the interaction between basic epitopes (NLRRITRVN, SHHGLHSTPD) and diverse acidic and aromatic-rich peptides using both MALDI and ESI Mass spectrometry. We show that adjacent histidines can also form stable noncovalent bonds and that those bonds are probably formed by a salt bridge between the phosphate or the acid residues and the histidines. However, noncovalent complexes with the arginine epitopes form more readily and are stronger than those with histidine-containing epitopes.
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Ehrenstorfer-Schäfers, Eva, Helmut Hartl, and Wolfgang Beck. "Bildung wasserlöslicher Histidin-Platin- Komplexe aus metallischem Platin und Histidin / Formation of Water Soluble Histidine Platinum Complexes from Metallic Platinum and Histidine." Zeitschrift für Naturforschung B 43, no. 4 (April 1, 1988): 499–500. http://dx.doi.org/10.1515/znb-1988-0421.
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AbstractMetallic Platinum dissolves under oxygen atmosphere in aqueous histidine solution. About 0.1 to 0.3 μmol of a water soluble histidine platinum complex per ml solution have been found by atomic absorption spectroscopy.
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Meena, Chhuttan L., Shubdha Ingole, Satyendra Rajpoot, Avinash Thakur, Prajwal P. Nandekar, Abhay T. Sangamwar, Shyam S. Sharma, and Rahul Jain. "Discovery of a low affinity thyrotropin-releasing hormone (TRH)-like peptide that exhibits potent inhibition of scopolamine-induced memory impairment in mice." RSC Advances 5, no. 70 (2015): 56872–84. http://dx.doi.org/10.1039/c5ra06935a.
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Remø, S. C., E. M. Hevrøy, P. A. Olsvik, R. Fontanillas, O. Breck, and R. Waagbø. "Dietary histidine requirement to reduce the risk and severity of cataracts is higher than the requirement for growth in Atlantic salmon smolts, independently of the dietary lipid source." British Journal of Nutrition 111, no. 10 (February 27, 2014): 1759–72. http://dx.doi.org/10.1017/s0007114513004418.
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The present study was carried out to investigate whether the dietary histidine requirement to reduce cataract development is higher than that for growth in Atlantic salmon smolts (Salmo salarL.) after seawater transfer and whether dietary vegetable oils contribute to cataractogenesis. Duplicate groups of salmon smolts were fed ten experimental diets with either fish oil (FO) or a vegetable oil (VO) mix replacing 70 % FO and histidine at five target levels (10, 12, 14, 16 and 18 g His/kg diet) for 13 weeks after seawater transfer. The VO diet-fed fish exhibited somewhat inferior growth and feed intakes compared with the FO diet-fed fish, irrespective of the dietary histidine concentration. Both cataract prevalence and severity were negatively correlated with the dietary histidine concentration, while lensN-acetyl-histidine (NAH) concentrations were positively correlated with it. The fatty acid profiles of muscle, heart and lens reflected that of the dietary oils to a descending degree and did not affect the observed cataract development. Muscle, heart and brain histidine concentrations reflected dietary histidine concentrations, while the corresponding tissue imidazole (anserine, carnosine and NAH) concentrations appeared to saturate differently with time. The expression level of liver histidase was not affected by the dietary histidine concentration, while the liver antioxidant response was affected in the VO diet-fed fish on a transcriptional level. The lowest severity of cataracts could be achieved by feeding 13·4 g His/kg feed, independently of the dietary lipid source. However, the present study also suggests that the dietary histidine requirement to minimise the risk of cataract development is 14·4 g His/kg feed.
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GHAZALEH, Faika A., George A. OMBURO, and Robert W. COLMAN. "Evidence for the presence of essential histidine and cysteine residues in platelet cGMP-inhibited phosphodiesterase." Biochemical Journal 317, no. 2 (July 15, 1996): 495–501. http://dx.doi.org/10.1042/bj3170495.
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cAMP is a major regulator of platelet function. cGMP-inhibited phosphodiesterase (cGI-PDE) is the predominant platelet enzyme hydrolysing cAMP. The pH–rate profile plot for this enzyme yields pKa values of 6.5 and 9.0, consistent with histidine and cysteine residues respectively. Diethyl pyrocarbonate (DEP) inactivates cGI-PDE in a time- and concentration-dependent manner, and this effect was rapidly reversed by hydroxylamine. It was estimated that 2 mol of histidine residues per mol of enzyme were responsible for the loss of catalytic activity, as deduced from the correlation of the difference spectrum at 240 nm of the DEP-modified cGI-PDE with the enzymic activity. N-Ethylmaleimide (NEM) and 5,5´-dithiobis-(2-nitrobenzoic acid) (DTNB) inactivate cGI-PDE in a time- and concentration-dependent manner, suggesting the selective modification of a cysteine residue. AMP protects the enzyme against DEP, NEM and DTNB, suggesting the presence of histidine and cysteine residues at the active site of cGI-PDE. [14C]DEP incorporation in the presence of AMP or cGMP indicates the protection of two histidine residues by each nucleotide. These residues are different for each agent, since the combination of AMP and cGMP protects four histidine residues. [3H]NEM incorporation showed that 1 mol of cysteine per mol of cGI-PDE was protected by AMP, but not by cGMP. We conclude that cGI-PDE possesses two essential histidine residues for activity, two additional histidines for cGMP inhibition, and one cysteine residue at the active site.
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Malinovsky, A. "Special features of histidine metabolism with different kinds of animals." Genetics and breeding of animals, no. 3 (November 17, 2023): 103–9. http://dx.doi.org/10.31043/2410-2733-2023-3-103-109.
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Natural amino acids being a part of food protein are known to be divided into essential and non-essential; essential ones if they are not present in food cannot be synthesized. There are two amino acids, threonine and histidine, which up to the present time have been a mystery for the biochemical science. However, it is universally recognized that threonine can be referred to as an essential amino acid as its absence from the food of all vertebrates results in the negative nitrogen balance. That is why specific features of threonine transformation with reference to different kinds of animals are not dealt with in the present paper. At the same time it was as far back as the thirties of the XX century that the fact of histidine being an essential amino acid for rats, mice, dogs and chickens but non-essential for men was proved. On the basis of the histidine essentiality thesis, a steady viewpoint that every living thing is not capabale of histidine synthesis was formed. But in this case the question arises: in what way has histidine become a non-essential amino acid for a healthy adult whereas for children and patients suffering from nephritic problems it has remained an essential amino acid? In view of the above different theories were put forward: 1) histidine reserves in haemoglobin and carnisone; the latter is enough with reference to adults but insufficient with reference to children; 2) histidine synthesis is caused by intestinal bacteria. But except mice whose muscles do not contain carnosine, the latter is a source of histidine for rats and dogs, histidine being an essential amino acid. It is only in the XXI century that the discovery of histidinol dehydrogenase enzyme has allowed to answer the question. Histidine essentiality / non-essentiality as well as any other amino acid should be taken into account when making up rations for people and agricultural animal.
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Myllylä, R., V. Günzler, K. I. Kivirikko, and D. D. Kaska. "Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl pyrocarbonate. Evidence for histidine residues in the catalytic site of 2-oxoglutarate-coupled dioxygenases." Biochemical Journal 286, no. 3 (September 15, 1992): 923–27. http://dx.doi.org/10.1042/bj2860923.
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A search for conserved amino acid residues within the cDNA-derived amino acid sequences of 2-oxoglutarate-coupled dioxygenases revealed the presence of two distinct motifs, spaced 49-71 amino acids apart, toward the C-terminal regions of these proteins. Each of the two common motifs contains an invariant histidine residue at a conserved position. The 2-oxoglutarate-coupled dioxygenases function in diverse processes, including the post-translational hydroxylation of proline and lysine residues in vertebrate collagens and the biosynthesis of microbial cephalosporins, yet they have a common reaction mechanisms, which requires the binding of Fe2+, 2-oxoglutarate, O2 and ascorbate at the catalytic site. The two regions of homology, and specifically the identical histidines, potentially represent functionally important sites related to their catalytic activity. Modification of histidine residues by diethyl pyrocarbonate inactivated vertebrate and algal prolyl 4-hydroxylase and vertebrate lysyl hydroxylase, indicating that histidine residues function in the catalytic site of these 2-oxoglutarate-coupled dioxygenases. Inactivation was prevented by the presence of co-substrates, but not by the peptide substrate. It is proposed that the histidine residues in the conserved motifs may function as Fe(2+)-binding ligands.
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Gaber, R. F., M. C. Kielland-Brandt, and G. R. Fink. "HOL1 mutations confer novel ion transport in Saccharomyces cerevisiae." Molecular and Cellular Biology 10, no. 2 (February 1990): 643–52. http://dx.doi.org/10.1128/mcb.10.2.643-652.1990.
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Saccharomyces cerevisiae histidine auxotrophs are unable to use L-histidinol as a source of histidine even when they have a functional histidinol dehydrogenase. Mutations in the hol1 gene permit growth of His- cells on histidinol by enhancing the ability of cells to take up histidinol from the medium. Second-site mutations linked to HOL1-1 further increase histidinol uptake. HOL1 double mutants and, to a lesser extent, HOL1-1 single mutants show hypersensitivity to specific cations added to the growth medium, including Na+, Li+, Cs+, Be2+, guanidinium ion, and histidinol, but not K+, Rb+, Ca2+, or Mg2+. The Na(+)-hypersensitive phenotype is correlated with increased uptake and accumulation of this ion. The HOL1-1-101 gene was cloned and used to generate a viable haploid strain containing a hol1 deletion mutation (hol1 delta). The uptake of cations, the dominance of the mutant alleles, and the relative inability of hol1 delta cells to take up histidinol or Na+ suggest that hol1 encodes an ion transporter. The novel pattern of ion transport conferred by HOL1-1 and HOL1-1-101 mutants may be explained by reduced selectivity for the permeant ions.
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Gaber, R. F., M. C. Kielland-Brandt, and G. R. Fink. "HOL1 mutations confer novel ion transport in Saccharomyces cerevisiae." Molecular and Cellular Biology 10, no. 2 (February 1990): 643–52. http://dx.doi.org/10.1128/mcb.10.2.643.
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Saccharomyces cerevisiae histidine auxotrophs are unable to use L-histidinol as a source of histidine even when they have a functional histidinol dehydrogenase. Mutations in the hol1 gene permit growth of His- cells on histidinol by enhancing the ability of cells to take up histidinol from the medium. Second-site mutations linked to HOL1-1 further increase histidinol uptake. HOL1 double mutants and, to a lesser extent, HOL1-1 single mutants show hypersensitivity to specific cations added to the growth medium, including Na+, Li+, Cs+, Be2+, guanidinium ion, and histidinol, but not K+, Rb+, Ca2+, or Mg2+. The Na(+)-hypersensitive phenotype is correlated with increased uptake and accumulation of this ion. The HOL1-1-101 gene was cloned and used to generate a viable haploid strain containing a hol1 deletion mutation (hol1 delta). The uptake of cations, the dominance of the mutant alleles, and the relative inability of hol1 delta cells to take up histidinol or Na+ suggest that hol1 encodes an ion transporter. The novel pattern of ion transport conferred by HOL1-1 and HOL1-1-101 mutants may be explained by reduced selectivity for the permeant ions.
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le Coq, Dominique, Sabine Fillinger, and Stéphane Aymerich. "Histidinol Phosphate Phosphatase, Catalyzing the Penultimate Step of the Histidine Biosynthesis Pathway, Is Encoded byytvP (hisJ) in Bacillus subtilis." Journal of Bacteriology 181, no. 10 (May 15, 1999): 3277–80. http://dx.doi.org/10.1128/jb.181.10.3277-3280.1999.
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ABSTRACT The deduced product of the Bacillus subtilis ytvP gene is similar to that of ORF13, a gene of unknown function in the Lactococcus lactis histidine biosynthesis operon. AB. subtilis ytvP mutant was auxotrophic for histidine. The only enzyme of the histidine biosynthesis pathway that remained uncharacterized in B. subtilis was histidinol phosphate phosphatase (HolPase), catalyzing the penultimate step of this pathway. HolPase activity could not be detected in crude extracts of the ytvP mutant, while purified glutathione S-transferase-YtvP fusion protein exhibited strong HolPase activity. These observations demonstrated that HolPase is encoded by ytvP inB. subtilis and led us to rename this genehisJ. Together with the HolPase of Saccharomyces cerevisiae and the presumed HolPases ofL. lactis and Schizosaccharomyces pombe, HisJ constitutes a family of related enzymes that are not homologous to the HolPases of Escherichia coli, Salmonella typhimurium, and Haemophilus influenzae.
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Sun, Wenqiang, Mengze Li, Hanjun Ren, Yang Chen, Wei Zeng, Xiong Tan, Xianbo Jia, Shiyi Chen, Jie Wang, and Songjia Lai. "Comparative Metabolomic Profiling of L-Histidine and NEFA Treatments in Bovine Mammary Epithelial Cells." Animals 14, no. 7 (March 29, 2024): 1045. http://dx.doi.org/10.3390/ani14071045.
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Non-esterified fatty acids (NEFAs) are pivotal in energy metabolism, yet high concentrations can lead to ketosis, a common metabolic disorder in cattle. Our laboratory observed lower levels of L-histidine in cattle suffering from ketosis, indicating a potential interaction between L-histidine and NEFA metabolism. This relationship prompted us to investigate the metabolomic alterations in bovine mammary epithelial cells (BMECs) induced by elevated NEFA levels and to explore L-histidine’s potential mitigating effects. Our untargeted metabolomic analysis revealed 893 and 160 metabolite changes in positive and negative models, respectively, with VIP scores greater than 1 and p-values below 0.05. Notable metabolites like 9,10-epoxy-12-octadecenoic acid were upregulated, while 9-Ethylguanine was downregulated. A pathway analysis suggested disruptions in fatty acid and steroid biosynthesis pathways. Furthermore, L-histidine treatment altered 61 metabolites in the positive model and 34 in the negative model, with implications for similar pathways affected by NEFA. Overlaying differential metabolites from both conditions uncovered a potential key mediator, 1-Linoleoylglycerophosphocholine, which was regulated in opposite directions by NEFA and L-histidine. Our study uncovered that both NEFA L- and histidine metabolomics analyses pinpoint similar lipid biosynthesis pathways, with 1-Linoleoylglycerophosphocholine emerging as a potential key metabolite mediating their interaction, a discovery that may offer insights for therapeutic strategies in metabolic diseases.
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Pogostin, Brett H., Anders Malmendal, Casey H. Londergan, and Karin S. Åkerfeldt. "pKa Determination of a Histidine Residue in a Short Peptide Using Raman Spectroscopy." Molecules 24, no. 3 (January 23, 2019): 405. http://dx.doi.org/10.3390/molecules24030405.
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Determining the pKa of key functional groups is critical to understanding the pH-dependent behavior of biological proteins and peptide-based biomaterials. Traditionally, 1H NMR spectroscopy has been used to determine the pKa of amino acids; however, for larger molecules and aggregating systems, this method can be practically impossible. Previous studies concluded that the C-D stretches in Raman are a useful alternative for determining the pKa of histidine residues. In this study, we report on the Raman application of the C2-D probe on histidine’s imidazole side chain to determining the pKa of histidine in a short peptide sequence. The pKa of the tripeptide was found via difference Raman spectroscopy to be 6.82, and this value was independently confirmed via 1H NMR spectroscopy on the same peptide. The C2-D probe was also compared to other Raman reporters of the protonation state of histidine and was determined to be more sensitive and reliable than other protonation-dependent signals. The C2-D Raman probe expands the tool box available to chemists interested in directly interrogating the pKa’s of histidine-containing peptide and protein systems.
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VANGURI, Vijay K., Shuxia WANG, Svetlana GODYNA, Sripriya RANGANATHAN, and Gene LIAU. "Thrombospondin-1 binds to polyhistidine with high affinity and specificity." Biochemical Journal 347, no. 2 (April 10, 2000): 469–73. http://dx.doi.org/10.1042/bj3470469.
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Thrombospondin-1 (TSP1) is a secreted trimeric glycoprotein of 450 kDa with demonstrated effects on cell growth, adhesion and migration. Its complex biological activity is attributed to its ability to bind to cell-surface receptors, growth factors and extracellular-matrix proteins. In this study, we used a 125I solid-phase binding assay to demonstrate that TSP1 binds specifically to proteins containing polyhistidine stretches. Based on studies with three different six-histidine-containing recombinant proteins, we derived an average dissociation constant of 5 nM. The binding of 125I-labelled TSP1 to these proteins was inhibited by peptides containing histidine residues, with the degree of competition being a function of the number of histidines within the peptide. Binding was not inhibited by excess histidine or imidazole, indicating that the imidazole ring is not sufficient for recognition by TSP1. Heparin was a potent inhibitor of binding with a Ki of 50 nM, suggesting that the heparin-binding domain of TSP1 may be involved in this interaction. This was confirmed by the ability of a recombinant heparin-binding domain of TSP1 to directly compete for TSP1 binding to polyhistidine-containing proteins. Affinity chromatography with a polyhistidine-containing peptide immobilized on agarose revealed that TSP1 in platelet releasates is the major polypeptide retained on the six-histidine-peptide column. We conclude that TSP1 contains a high-affinity binding site for polyhistidine and this is likely to be the molecular basis for the observed binding of TSP1 to histidine-rich glycoprotein. The possibility that other polyhistidine-containing proteins also interact with TSP1 warrants further study.
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Nawłoka, Paulina, Małgorzata Kalinowska, Cezary Paczkowski, and Zdzisław A. Wojciechowski. "Evidence for essential histidine and dicarboxylic amino-acid residues in the active site of UDP-glucose : solasodine glucosyltransferase from eggplant leaves." Acta Biochimica Polonica 50, no. 2 (June 30, 2003): 567–72. http://dx.doi.org/10.18388/abp.2003_3710.
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Effects of several chemical probes selectively modifying various amino-acid residues on the activity of UDP-glucose : solasodine glucosyltransferase from eggplant leaves was studied. It was shown that diethylpyrocarbonate (DEPC), a specific modifier of histidine residues, was strongly inhibitory. However, in the presence of excessive amounts of the enzyme substrates, i.e. either UDP-glucose or solasodine, the inhibitory effect of DEPC was much weaker indicating that histidine (or histidines) are present in the active site of the enzyme. Our results suggest also that unmodified residues of glutamic (or aspartic) acid, lysine, cysteine, tyrosine and tryptophan are necessary for full activity of the enzyme. Reagents modifying serine and arginine residues have no effect on the enzyme activity.
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Boncompagni, Eric, Laurence Dupont, Tam Mignot, Magne Østeräs, Annie Lambert, Marie-Christine Poggi, and Daniel Le Rudulier. "Characterization of a Sinorhizobium melilotiATP-Binding Cassette Histidine Transporter Also Involved in Betaine and Proline Uptake." Journal of Bacteriology 182, no. 13 (July 1, 2000): 3717–25. http://dx.doi.org/10.1128/jb.182.13.3717-3725.2000.
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ABSTRACT The symbiotic soil bacterium Sinorhizobium melilotiuses the compatible solutes glycine betaine and proline betaine for both protection against osmotic stress and, at low osmolarities, as an energy source. A PCR strategy based on conserved domains in components of the glycine betaine uptake systems from Escherichia coli(ProU) and Bacillus subtilis (OpuA and OpuC) allowed us to identify a highly homologous ATP-binding cassette (ABC) binding protein-dependent transporter in S. meliloti. This system was encoded by three genes (hutXWV) of an operon which also contained a fourth gene (hutH2) encoding a putative histidase, which is an enzyme involved in the first step of histidine catabolism. Site-directed mutagenesis of the gene encoding the periplasmic binding protein (hutX) and of the gene encoding the cytoplasmic ATPase (hutV) was done to study the substrate specificity of this transporter and its contribution in betaine uptake. These mutants showed a 50% reduction in high-affinity uptake of histidine, proline, and proline betaine and about a 30% reduction in low-affinity glycine betaine transport. When histidine was used as a nitrogen source, a 30% inhibition of growth was observed inhut mutants (hutX and hutH2). Expression analysis of the hut operon determined using ahutX-lacZ fusion revealed induction by histidine, but not by salt stress, suggesting this uptake system has a catabolic role rather than being involved in osmoprotection. To our knowledge, Hut is the first characterized histidine ABC transporter also involved in proline and betaine uptake.
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Afrose, Fahmida, and Roger E. Koeppe II. "Comparing Interfacial Trp, Interfacial His and pH Dependence for the Anchoring of Tilted Transmembrane Helical Peptides." Biomolecules 10, no. 2 (February 11, 2020): 273. http://dx.doi.org/10.3390/biom10020273.
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Charged and aromatic amino acid residues, being enriched toward the terminals of membrane-spanning helices in membrane proteins, help to stabilize particular transmembrane orientations. Among them, histidine is aromatic and can be positively charge at low pH. To enable investigations of the underlying protein-lipid interactions, we have examined the effects of single or pairs of interfacial histidine residues using the constructive low-dynamic GWALP23 (acetyl-GG2ALW5LALALALALALALW19LAG22A-amide) peptide framework by incorporating individual or paired histidines at locations 2, 5, 19 or 22. Analysis of helix orientation by means of solid-state 2H NMR spectra of labeled alanine residues reveals marked differences with H2,22 compared to W2,22. Nevertheless, the properties of membrane-spanning H2,22WALP23 helices show little pH dependence and are similar to those having Gly, Arg or Lys at positions 2 and 22. The presence of H5 or H19 influences the helix rotational preference but not the tilt magnitude. H5 affects the helical integrity, as residue 7 unwinds from the core helix; yet once again the helix orientation and dynamic properties show little sensitivity to pH. The overall results reveal that the detailed properties of transmembrane helices depend upon the precise locations of interfacial histidine residues.
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Kern, Melanie, Juliane Scheithauer, Robert G. Kranz, and Jörg Simon. "Essential histidine pairs indicate conserved haem binding in epsilonproteobacterial cytochrome c haem lyases." Microbiology 156, no. 12 (December 1, 2010): 3773–81. http://dx.doi.org/10.1099/mic.0.042838-0.
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Bacterial cytochrome c maturation occurs at the outside of the cytoplasmic membrane, requires transport of haem b across the membrane, and depends on membrane-bound cytochrome c haem lyase (CCHL), an enzyme that catalyses covalent attachment of haem b to apocytochrome c. Epsilonproteobacteria such as Wolinella succinogenes use the cytochrome c biogenesis system II and contain unusually large CCHL proteins of about 900 amino acid residues that appear to be fusions of the CcsB and CcsA proteins found in other bacteria. CcsBA-type CCHLs have been proposed to act as haem transporters that contain two haem b coordination sites located at different sides of the membrane and formed by histidine pairs. W. succinogenes cells contain three CcsBA-type CCHL isoenzymes (NrfI, CcsA1 and CcsA2) that are known to differ in their specificity for apocytochromes and apparently recognize different haem c binding motifs such as CX2CH (by CcsA2), CX2CK (by NrfI) and CX15CH (by CcsA1). In this study, conserved histidine residues were individually replaced by alanine in each of the W. succinogenes CCHLs. Characterization of NrfI and CcsA1 variants in W. succinogenes demonstrated that a set of four histidines is essential for maturing the dedicated multihaem cytochromes c NrfA and MccA, respectively. The function of W. succinogenes CcsA2 variants produced in Escherichia coli was also found to depend on each of these four conserved histidine residues. The presence of imidazole in the growth medium of both W. succinogenes and E. coli rescued the cytochrome c biogenesis activity of most histidine variants, albeit to different extents, thereby implying the presence of two functionally distinct histidine pairs in each CCHL. The data support a model in which two conserved haem b binding sites are involved in haem transport catalysed by CcsBA-type CCHLs.
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van Milgen, Jaap, and Nathalie Le Floc’h. "8 Functional Role of Histidine in Diets of Young Pigs." Journal of Animal Science 99, Supplement_1 (May 1, 2021): 13. http://dx.doi.org/10.1093/jas/skab054.022.
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Abstract Histidine is a constituent amino acid of body proteins and, once incorporated in protein, histidine can be methylated post-translationally to methyl-histidine. Histidine is also a precursor of histamine, a neurotransmitter and involved in the immune response. Histidine and histamine are constituents of a number of dipeptides, which act as pH buffers, metal chelating agents, and anti-oxidants, especially in skeletal muscles and in the brain. A considerable fraction of whole-body histidine is present as carnosine, the dipeptide of histidine and β-alanine. In the longissimus muscle, about 40% of the total histidine content is present as carnosine. The histidine in carnosine can be methylated to anserine or balenine, and the pig is among the few species that synthesize both forms. Hydrolysis of body protein and of histidine-containing dipeptides results in the release of the constituent amino acids. However, only the histidine of protein and carnosine can be reused for protein synthesis. Methyl-histidine is either excreted in the urine or remains bound in the dipeptides and accumulates in the body. Because carnosine represents such a large histidine reservoir, a dietary histidine deficiency may not directly lead to a reduction in growth, especially if growth is given a higher priority for histidine utilization than maintaining or depleting the histidine-containing dipeptide reserves. Few histidine dose-response studies have been done in piglets and differences in the estimated requirements may be due to differences in diluting or depleting the dipeptide reserves. However, at low histidine intakes, both feed intake and growth are reduced and a reduction of the histidine-to-lysine supply by 1 percentage point results in a growth reduction of 4%. Histidine dose-response studies need to consider the role of histidine as a constituent amino acid of body protein as well as its role in dipeptides.
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Cianciaruso, B., S. Fukuda, M. R. Jones, and J. D. Kopple. "Net release or uptake of histidine and carnosine in kidney of dogs." American Journal of Physiology-Endocrinology and Metabolism 248, no. 1 (January 1, 1985): E51—E57. http://dx.doi.org/10.1152/ajpendo.1985.248.1.e51.
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Previous studies are equivocal as to whether the dog kidney produces histidine. Because one possible source of renal histidine is carnosine (beta-alanyl-L-histidine), we investigated net renal production (release) or utilization (uptake) (Qmet) of histidine and carnosine in 19 female dogs after they were fed histidine-free (9 dogs) or histidine-containing diets (10 dogs). Diets were fed in short-(2-11 days) or long-term (52-57 days) studies. Dogs were infused with half-normal saline for 120 min followed by an infusion of half-normal saline containing carnosine, 50 mumol/min. Renal Qmet histidine, calculated from either plasma or whole blood values, was positive during infusion of half-normal saline. During carnosine infusion, Qmet histidine increased markedly, and there was net renal uptake of carnosine. The Qmet histidine and carnosine were not different in the dogs fed histidine-free vs. histidine-containing diets. Thus there is net renal release of histidine in female dogs that increases when carnosine is administered. Qmet histidine or carnosine do not change adaptively when dogs are fed histidine-free diets.
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Ingle, Robert A. "Histidine Biosynthesis." Arabidopsis Book 9 (January 2011): e0141. http://dx.doi.org/10.1199/tab.0141.
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Ginsburg, Isaac, Ruth Borinski, Milu Sadovnic, Yael Eilam, and Kim Rainsford. "Polyl-histidine." Inflammation 11, no. 3 (September 1987): 253–77. http://dx.doi.org/10.1007/bf00915832.
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Stellwagen, Nancy C., Cecilia Gelfi, and Pier Giorgio Righetti. "DNA–histidine complex formation in isoelectric histidine buffers." Journal of Chromatography A 838, no. 1-2 (April 1999): 179–89. http://dx.doi.org/10.1016/s0021-9673(99)00049-7.
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Shen, C., L. Yang, S. L. Miller, and J. Oro. "The prebiotic synthesis of histidine and histidyl-histidine." Origins of Life and Evolution of the Biosphere 19, no. 3-5 (May 1989): 258–59. http://dx.doi.org/10.1007/bf02388839.
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Thalacker-Mercer, Anna E., and Mary E. Gheller. "Benefits and Adverse Effects of Histidine Supplementation." Journal of Nutrition 150, Supplement_1 (October 1, 2020): 2588S—2592S. http://dx.doi.org/10.1093/jn/nxaa229.
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ABSTRACT Histidine is a nutritionally essential amino acid with many recognized benefits to human health, while circulating concentrations of histidine decline in pathologic conditions [e.g., chronic obstructive pulmonary disease (COPD) and chronic kidney disease (CKD)]. The purpose of this review is to examine the existing literature regarding the benefits of histidine intake, the adverse effects of excess histidine, and the upper tolerance level for histidine. Supplementation with doses of 4.0–4.5 g histidine/d and increased dietary histidine intake are associated with decreased BMI, adiposity, markers of glucose homeostasis (e.g., HOMA-IR, fasting blood glucose, 2-h postprandial blood glucose), proinflammatory cytokines, and oxidative stress. It is unclear from the limited number of studies in humans whether the improvements in glucoregulatory markers, inflammation, and oxidative stress are due to reduced BMI and adiposity, increased carnosine (a metabolic product of histidine with antioxidant effects), or both. Histidine intake also improves cognitive function (e.g., reduces appetite, anxiety, and stress responses and improves sleep) potentially through the metabolism of histidine to histamine; however, this relation is ambiguous in humans. At high intakes of histidine (>24 g/d), studies report adverse effects of histidine such as decreased serum zinc and cognitive impairment. There is limited research on the effects of histidine intake at doses between 4.5 and 24 g/d, and thus, a tolerable upper level has not been established. Determining tolerance to histidine supplementation has been limited by small sample sizes and, more important, a lack of a clear biomarker for histidine supplementation. The U-shaped curve of circulating zinc concentrations with histidine supplementation could be exploited as a relevant biomarker for supplemental histidine tolerance. Histidine is an important amino acid and may be necessary as a supplement in some populations; however, gaps in knowledge, which this review highlights, need to be addressed scientifically.
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Ramage, Elizabeth, Larry Gallagher, and Colin Manoil. "Exploiting a Natural Auxotrophy for Genetic Selection." Applied and Environmental Microbiology 78, no. 16 (June 1, 2012): 5926–28. http://dx.doi.org/10.1128/aem.00762-12.
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ABSTRACTWe exploited the natural histidine auxotrophy ofFrancisellaspecies to develophisD(encodes histidinol dehydrogenase) as a positive selection marker. A shuttle plasmid (pBR103) carryingEscherichia coli hisDand designed for cloning of PCR fragments replicated in both attenuated and highly virulentFrancisellastrains. During this work, we formulated a simplified defined growth medium forFrancisella novicida.
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WRAGG, Stephanie, K. Fred HAGEN, and A. Lawrence TABAK. "Identification of essential histidine residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1." Biochemical Journal 328, no. 1 (November 15, 1997): 193–97. http://dx.doi.org/10.1042/bj3280193.
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UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGaNTases) catalyse the initial step of mucin-type O-glycosylation. The activity of bovine ppGaNTase-T1 isoenzyme was inhibited by diethyl pyrocarbonate (DEPC) modification. Activity was partially restored by hydroxylamine treatment, indicating that one of the reactive residues was a histidine. The transferase was protected against DEPC inactivation when UDP-GalNAc and EPO-G, a peptide pseudo-substrate PPDAAGAAPLR, were simultaneously present, while presence of EPO-G alone did not alter DEPC inactivation. However, inclusion of UDP-GalNAc alone potentiated DEPC-inhibition of the enzyme, suggesting that UDP-GalNAc binding changes the accessibility or reactivity of an essential histidine residue. Deletion of the first 56 amino acids (including one hisitidine residue) yielded a fully active secreted form of the bovine ppGaNTase-T1 enzyme. Each of the 14 remaining histidines in the enzyme were mutated to alanine, and the recombinant mutants were recovered from COS7 cells. The mutation of histidine residues His211 → Ala and His344 → Ala resulted in recombinant proteins with no detectable enzymic activity. A significant decrease in the initial rate of GalNAc transfer to the substrate was observed with mutants His125 → Ala and His341 → Ala (1% and 6% of wild-type activity respectively). Mutation of the remaining ten histidine residues yielded mutants that were indistinguishable from the wild-type enzyme. Mutagenesis and SDS/PAGE analysis of all N-glycosylation sequons revealed that positions N-95 and N-552 are occupied by N-linked sugars in COS7 cells. Ablation of either site did not perturb enzyme biosynthesis or enzyme activity.
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Rodnin, Mykola V., Victor Vasques-Montes, Alexander Kyrychenko, Nuno F. B. Oliveira, Maithri M. Kashipathy, Kevin P. Battaile, Justin Douglas, Scott Lovell, Miguel Machuqueiro, and Alexey S. Ladokhin. "Histidine Protonation and Conformational Switching in Diphtheria Toxin Translocation Domain." Toxins 15, no. 7 (June 25, 2023): 410. http://dx.doi.org/10.3390/toxins15070410.
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Protonation of key histidine residues has been long implicated in the acid-mediated cellular action of the diphtheria toxin translocation (T-) domain, responsible for the delivery of the catalytic domain into the cell. Here, we use a combination of computational (constant-pH Molecular Dynamics simulations) and experimental (NMR, circular dichroism, and fluorescence spectroscopy along with the X-ray crystallography) approaches to characterize the initial stages of conformational change happening in solution in the wild-type T-domain and in the H223Q/H257Q double mutant. This replacement suppresses the acid-induced transition, resulting in the retention of a more stable protein structure in solutions at pH 5.5 and, consequently, in reduced membrane-disrupting activity. Here, for the first time, we report the pKa values of the histidine residues of the T-domain, measured by NMR-monitored pH titrations. Most peaks in the histidine side chain spectral region are titrated with pKas ranging from 6.2 to 6.8. However, the two most up-field peaks display little change down to pH 6, which is a limiting pH for this protein in solution at concentrations required for NMR. These peaks are absent in the double mutant, suggesting they belong to H223 and H257. The constant-pH simulations indicate that for the T-domain in solution, the pKa values for histidine residues range from 3.0 to 6.5, with those most difficult to protonate being H251 and H257. Taken together, our experimental and computational data demonstrate that previously suggested cooperative protonation of all six histidines in the T-domain does not occur.
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Werner, Ekkehard, Anthony A. Holder, Andras Aszodi, and William R. Taylor. "A Novel 11-Residue Coiled-Coil Motif Predicts a Histidine Zipper." Protein & Peptide Letters 3, no. 2 (April 1996): 139–45. http://dx.doi.org/10.2174/092986650302220614124810.
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Abstract: A protein sequence is described that consists of a highly repeated 11-mer motif. The motif has the characteristics of an α -helical coilled-coil but contains, in addition, a highly conserved histidine position that lies centrally on the hydrophobic face of the amphipathic helix. The sequence was modelled as ei ther a three or four stranded coilled-coil with the histidines hydrogen-bonded . (like a zipper) in the core.
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Tanio, Michikazu, and Toshiyuki Kohno. "Histidine-regulated activity of M-ficolin." Biochemical Journal 417, no. 2 (December 23, 2008): 485–91. http://dx.doi.org/10.1042/bj20081640.
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Human M-ficolin is a pathogen-associated molecular recognition molecule in the innate immune system, and it binds to some sugars, such as GlcNAc (N-acetylglucosamine), on pathogen surfaces. From previous structural and functional studies of the FD1 (M-ficolin fibrinogen-like domain), we proposed that the ligand-binding region of FD1 exists in a conformational equilibrium between active and non-active states depending on three groups with a pKa of 6.2, which are probably histidine residues, and suggested that the 2-state conformational equilibrium as well as the trimer formation contributes to the discrimination mechanism between self and non-self of FD1 [Tanio, M., Kondo, S., Sugio, S. and Kohno, T. (2007) J. Biol. Chem. 282, 3889–3895]. To investigate the origins of the pH dependency, mutational analyses were performed on FD1 expressed by Brevibacillus choshinensis. The GlcNAc binding study of a series of single histidine mutants of FD1 demonstrated that His251, His284 and His297 are required for the activity, and thus we concluded that the three histidines are the origins of the pH dependency of FD1. Monomeric mutants of FD1 show weaker affinity for the ligand than the trimeric wild-type, indicating that trimer formation confers high avidity for the ligand. In addition, analyses of the GlcNAc association and dissociation of FD1 provided evidence that FD1 always exchanges between the active and non-active states with the pH-dependent populations in solution. The biological roles of the histidine-regulated conformational equilibrium of M-ficolin are discussed in terms of the self and non-self discrimination mechanism.
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Suresh, S., and M. Vijayan. "X-ray studies on crystalline complexes involving amino acids and peptides. XXX. Structural invariance and optical resolution through interactions with an achiral molecule in the histidine complexes of glycolic acid." Acta Crystallographica Section B Structural Science 52, no. 5 (October 1, 1996): 876–81. http://dx.doi.org/10.1107/s0108768196005368.
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The crystals of DL-histidine glycolate and L-histidine glycolate were prepared and analysed as part of an ongoing programme aimed at studying biologically and evolutionarily important interaction and aggregation Patterns. Crystallization experiments involving DL-histidine and glycolic acid yielded, in addition to DL-histidine glycolate, a conglomerate containing crystals of L-histidine glycolate and D-histidine glycolate in an unusual process of chiral separation through interaction with an achiral molecule. The crystal structure of DL-histidine glycolate is made up of alternating layers of unlike molecules as in many other binary complexes involving amino acids. The structure of L-histidine glycolate involves packing of columns containing L-histidine molecules and glycolate ions tightly hydrogen bonded to one another. The arrangement is almost identical to that in the structure of L-histidine acetate, thus providing another example for the invariance of certain aggregation patterns with respect to changes in the molecules involved. The observed aggregation of molecules in the chiral complex also appears to provide a structural rationale for chiral separation of histidine in the presence of glycolic acid.
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Gill, J. S., Y. Yiangou, D. J. Webb, L. Meleagros, N. Benjamin, B. J. Chrysanthou, J. R. Cockcroft, R. C. Causon, A. J. Camm, and S. R. Bloom. "Peptide histidine valine: Its haemodynamic actions and pharmacokinetics in man differ from those of vasoactive intestinal peptide and peptide histidine methionine." Clinical Science 78, no. 5 (May 1, 1990): 487–92. http://dx.doi.org/10.1042/cs0780487.
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1. The effects of intravenous and intra-arterial infusion of the peptides derived from prepro-vasoactive intestinal peptide, vasoactive intestinal peptide, peptide histidine methionine and peptide histidine valine, were examined in six healthy volunteers. 2. Vasoactive intestinal peptide given intravenously caused a significant increase in heart rate and a decrease in diastolic, but not systolic, blood presure, whereas peptide histidine valine caused an increase in heart rate alone, despite higher achieved circulating peptide concentrations. Peptide histidine methionine did not affect heart rate or blood pressure. Forearm blood flow was increased by vasoactive intestinal peptide and peptide histidine valine when infused locally intra-arterially, although vasoactive intestinal peptide was more potent than peptide histidine valine. 3. Plasma concentrations of cardiodilatin (the N-terminal peptide derived from pro-atrial natriuretic peptide) were increased by intravenous infusion of vasoactive intestinal peptide, but were unaffected by peptide histidine methionine or peptide histidine valine. Circulating plasma concentrations of adrenaline and noradrenaline did not change during infusion of vasoactive intestinal peptide, peptide histidine methionine or peptide histidine valine. 4. Peptide histidine valine had a long half-life when compared with peptide histidine methionine and vasoactive intestinal peptide. 5. We conclude that peptide histidine valine is active in the human cardiovascular system and has a similar, though less potent, vasodilating action to vasoactive intestinal peptide. The higher circulating levels of peptide histidine valine found in man suggest that it may be important in modulating vascular tone.
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Torres, Nimbe, Lariza Beristain, Hector Bourges, and Armando R. Tovar. "Histidine-Imbalanced Diets Stimulate Hepatic Histidase Gene Expression in Rats." Journal of Nutrition 129, no. 11 (November 1, 1999): 1979–83. http://dx.doi.org/10.1093/jn/129.11.1979.
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Teng, Henry, and Charles Grubmeyer. "Mutagenesis of Histidinol Dehydrogenase Reveals Roles for Conserved Histidine Residues†." Biochemistry 38, no. 22 (June 1999): 7363–71. http://dx.doi.org/10.1021/bi982758p.
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Li, Xinyi, Zezhou Li, and Meiping Zhao. "Illuminating Histidine-Deficient Intracellular Environments: A Novel Whole-Cell Microbial Fluorescence Sensor." Chemosensors 11, no. 10 (September 30, 2023): 515. http://dx.doi.org/10.3390/chemosensors11100515.
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Histidine is an essential amino acid with significant implications for human growth and neuromodulation. Its intracellular concentration, whether increased or decreased, can indicate different diseases. While various methods exist for measuring elevated histidine levels, there remains a significant lack of sensors capable of actively responding to histidine deficiency within cells and releasing strong signals. In this study, we exploited the high induction levels of the his operon in S. Typhimurium SL1344, a histidine auxotroph, within a histidine-deficient environment, to develop a specific bacterial sensor with sensitivity towards low histidine concentrations. By employing plasmid vectors with differing copy numbers, we developed two distinct bacterial fluorescence sensors, both capable of actively responding to histidine deficiency and emitting detectable fluorescence signals within either culture mediums or live cells. The SL1344-pGEX sensor, with a high copy number, exhibited remarkable sensitivity and selectivity to histidine in the range of 0 to 50 μM. Notably, even a minimal addition of histidine (approximately 2.5 μM) to the M9 medium led to observable fluorescence reduction, rendering it highly suitable for monitoring histidine-deficient cellular environments. In contrast, the low-copy-number SL1344-pSB3313 sensor exhibits a broader response range, capable of tracking more extensive shifts in histidine concentrations. These sensors allow for sensitive in situ detection of intracellular histidine concentrations in various live cells, particularly responding to real-time changes in cellular histidine levels. This provides a powerful tool for investigating histidine deficiency-related biological processes, the mechanisms of associated diseases, and the assessment and optimization of therapeutic strategies.
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Sakurai, Eiichi, Tomoya Sakurada, Yoshinori Ochiai, Jun Yamakami, and Yorihisa Tanaka. "Stereoselective transport of histidine in rat lung microvascular endothelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 282, no. 6 (June 1, 2002): L1192—L1197. http://dx.doi.org/10.1152/ajplung.00405.2001.
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The transport characteristics of l- and d-histidine through the blood-lung barrier were studied in cultured rat lung microvascular endothelial cells (LMECs). l-Histidine uptake was a saturable process. The addition of metabolic inhibitors [2,4-dinitrophenol (DNP) and rotenone] reduced the uptake rate ofl-histidine. Ouabain, an inhibitor of Na+-K+-ATPase, also reduced uptake ofl-histidine. Moreover, the initial l-histidine uptake rate was reduced by the substitution of Na+ with choline chloride and choline bicarbonate in the incubation buffer. The system N substrate, l-glutamic acid γ-monohydroxamate, also inhibited uptake of l-histidine. However, system N-mediated transport was not pH sensitive. These results demonstrated that l-histidine is actively taken up by a system N transport mechanism into rat LMECs, with energy supplied by Na+. Moreover, the Na+-independent system L substrate, 2-amino-2-norbornanecarboxylic acid (BCH), had an inhibitory effect on l-histidine uptake in Na+ removal, indicating facilitated diffusion by a Na+-independent system L transport into the rat LMECs. These results provide evidence for there being at least two pathways for l-histidine uptake into rat LMECs, a Na+-dependent system N and Na+-independent system L process. On the other hand, the uptake of d-histidine into rat LMECs was not reduced by the addition of DNP, rotenone, or ouabain, or by Na+replacement. Although the uptake of d-histidine was reduced in the presence of BCH, the addition of l-glutamic acid γ-monohydroxamate did not significantly decrease uptake ofd-histidine. These results suggest that the uptake ofd-histidine by rat LMECs has different characteristics compared with its isomer, l-histidine, indicating that system N transport did not involve d-histidine uptake.
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Kang, Meng, Jie Yin, Jie Ma, Xin Wu, Ke Huang, Tiejun Li, and Long Ouyang. "Effects of Dietary Histidine on Growth Performance, Serum Amino Acids, and Intestinal Morphology and Microbiota Communities in Low Protein Diet-Fed Piglets." Mediators of Inflammation 2020 (November 28, 2020): 1–7. http://dx.doi.org/10.1155/2020/1240152.
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Previous study showed that low protein diet-fed pigs are characterized by lower histidine concentration in the serum and muscle, suggesting that histidine may involve in protein-restricted response. Thus, the current study mainly investigated the effects of dietary histidine on growth performance, blood biochemical parameters and amino acids, intestinal morphology, and microbiota communities in low protein diet-challenged-piglets. The results showed that protein restriction inhibited growth performance, blood biochemical parameters and amino acids, and gut microbiota but had little effect on intestinal morphology. Dietary supplementation with histidine markedly enhanced serum histidine level and restored tryptophan concentration in low protein diet-fed piglets, while growth performance and intestinal morphology were not markedly altered in histidine-treated piglets. In addition, histidine exposure failed to affect bacterial diversity (observed species, Shannon, Simpson, Chao1, ACE, and phylogenetic diversity), but histidine-treated piglets exhibited higher abundances of Butyrivibrio and Bacteroides compared with the control and protein-restricted piglets. In conclusion, dietary histidine in low protein diet enhanced histidine concentration and affected gut microbiota (Butyrivibrio and Bacteroides) but failed to improve growth performance and intestinal morphology.
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Spinner, F., M. R. Cheesman, A. J. Thomson, T. Kaysser, R. B. Gennis, Q. Peng, and J. Peterson. "The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation." Biochemical Journal 308, no. 2 (June 1, 1995): 641–44. http://dx.doi.org/10.1042/bj3080641.
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The cytochrome bd ubiquinol oxidase from Escherichia coli is induced when the bacteria are cultured under microaerophilic or low-aeration conditions. This membrane-bound respiratory oxidase catalyses the two-electron oxidation of ubiquinol and the four-electron reduction of dioxygen to water. The oxidase contains three haem prosthetic groups: haem b558, haem b595 and haem d. Haem d is the oxygen binding site, and it is likely that haem d and b595 form a bimetallic site in the enzyme. Haem b558 has been previously characterized spectroscopically as being low spin and has been shown to be located within subunit I (CydA) of this two-subunit enzyme. It is likely that haem b558 is associated with the quinol oxidation site, which has also been shown to be within subunit I. In a previous effort to locate the specific amino acids axially ligated to haem b558, all six histidines within subunit I were altered by site-directed mutagenesis. Only one, histidine-186, was identified as a likely ligand to haem b558. Hence it was suggested that haem b558 could not have bis(histidine) ligation. In the current work, a combination of low-temperature near-infrared magnetic circular dichroism (NIR-MCD) and EPR spectroscopies have been employed to identify the nature of the haem b558 axial ligands. The NIR-MCD spectrum at cryogenic temperatures is dominated by the low-spin haem b558 component of the complex, and the low-energy band near 1800 nm is strong evidence for histidine-methionine ligation. It is concluded that haem b558 is ligated to histidine-186 plus one of the methionines located within subunit I of the oxidase.
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Hutson, R. G., and M. S. Kilberg. "Cloning of rat asparagine synthetase and specificity of the amino acid-dependent control of its mRNA content." Biochemical Journal 304, no. 3 (December 15, 1994): 745–50. http://dx.doi.org/10.1042/bj3040745.
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A full-length cDNA clone for rat asparagine synthetase (AS) was isolated from a cDNA library enriched for amino acid-regulated sequences. The AS cDNA was used to investigate the amino acid-dependent repression of AS mRNA content in rat Fao hepatoma cells. In response to complete amino acid starvation, there was an approximately 10-fold increase in the level of AS mRNA. Three species of mRNA, of approx. sizes 2.0, 2.5 and 4.0 kb, were detected and each was simultaneously regulated to the same degree. The expression of AS mRNA increased by 6 h after removal of amino acids, reached a plateau after 9 h, and was blocked by either actinomycin D or cycloheximide. Partial repression of the AS mRNA content was maintained by the presence of a single amino acid in the culture medium, but the degree of effectiveness for each one varied widely. Glutamine showed the greatest ability to repress the AS mRNA content, even at an extracellular concentration 10 times below its plasma level. Other effective repressors included the amino acids asparagine, histidine and leucine, as well as ammonia. Depletion of selected single amino acids from an otherwise complete culture medium also caused up-regulation. In particular, removal of histidine, threonine or tryptophan from the medium, or the addition of histidinol to inhibit histidinyl-tRNA synthetase, resulted in a significant increase in AS mRNA content. The data indicate that nutrient regulation of AS mRNA occurs by a general control mechanism that is responsive to a spectrum of amino acids.
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Cooperman, Jack M., and Rafael Lopez. "The Role of Histidine in the Anemia of Folate Deficiency." Experimental Biology and Medicine 227, no. 11 (December 2002): 998–1000. http://dx.doi.org/10.1177/153537020222701107.
Full textAbstract:
The amino acid histidine is metabolized to glutamic acid in mammalian tissue. Formiminoglutamic acid (FIGLU) is an intermediary in this reaction, and tetrahydrofolic acid is the coenzyme that converts it to glutamic acid. A test for folate deficiency concerns the measurement of urinary FIGLU excretion after a histidine load. It was observed that folate-deficient individuals receiving the histidine for the FIGLU test made hematological response that alleviated the anemia associated with this deficiency. This was unusual in that a biochemical test to determine the deficiency results in a beneficial effect for one aspect of the deficiency. The studies reported in this paper give a metabolic explanation for this phenomenon. Urine was collected for 24 hr from 25 folate-deficient subjects, 10 vitamin B12-deficient subjects, and 15 normal controls. Urinary excretion of histidine was a mean of 203 mg with a range of 130–360 mg for the folate-deficient subjects; 51.5 mg with a range of 30–76.6 mg for normal subjects; and 60.0 mg with a range of 32.3–93.0 mg for the vitamin B12-deficient subjects. All the folate-deficient subjects subsequently made a hematological response to the histidine administered for the FIGLU test. No hematological response was observed in the vitamin B12-deficient individuals. When folic acid was given to folate-deficient subjects who received no histidine, urinary histidine levels returned to normal levels rapidly and this was followed by a hematological response. Others have shown that volunteers fed a histidine-free diet developed anemia. In normal subjects, histidine is excreted much more in the urine than other essential amino acids are. Hemoglobin protein contains 10% histidine. Under normal conditions, dietary histidine can supply sufficient histidine to prevent anemia. When the dietary intake is diminished or the urinary excretion is greatly increased, anemia results. It is concluded that folate deficiency causes histidine depletion through increased urinary excretion of this amino acid. Feeding histidine replenishes tissue levels of histidine, resulting in hemoglobin regeneration. Folic acid administration results in return of histidine to normal urinary levels. Thus, a combination of folic acid histidine would be beneficial for folate deficient individuals.
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Quam, Darcy D., James G. Morris, and Quinton R. Rogers. "Histidine requirement of kittens for growth, haematopoiesis and prevention of cataracts." British Journal of Nutrition 58, no. 3 (November 1987): 521–32. http://dx.doi.org/10.1079/bjn19870120.
Full textAbstract:
1. The histidine requirement of growing kittens was determined from an experiment in which forty-eight kittens were randomly allocated to six amino acid-based diets supplying: 1.0, 1.5, 2.0, 2.5, 3.0 or 4.5 g histidine base/kg diet.2. By 48 d it was obvious that 1.0 and 1.5 g histidine/kg diet were grossly inadequate so the kittens receiving these two diets were removed from the experiment. The other four groups of kittens continued to receive their diets for a total of 128 d.3. Mean daily weight gain, nitrogen retention and food intake attained plateau values at 2.1 g histidine/kg diet.4. Blood samples taken at 25 and 48 d after kittens were given the diets showed a significant effect of dietary histidine on haemoglobin (Hb) concentration. Hb and packed cell volume (PCV) attained asymptotic values at 3.0 g histidine/kg diet at 48 d. At 128 d, kittens consuming diets containing 2.0–4.5 g histidine/kg had similar Hb and PCV values.5. Cataracts of both eyes were observed in two of nine female kittens which had received diets containing either 2.0 or 2.5 g histidine/kg.6. A concentration of 3 g histidine/kg diet is recommended as a practical guide for feeding kittens.7. There was a rectilinear relation (r2 0.99) between the logarithm of the histidine concentration of plasma and the concentrationof histidine in the diet over the range 1.5–3.0 g histidine/kg diet.
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Rossetto, O., G. Schiavo, P. Polverino de Laureto, S. Fabbiani, and C. Montecucco. "Surface topography of histidine residues of tetanus toxin probed by immobilized-metal-ion affinity chromatography." Biochemical Journal 285, no. 1 (July 1, 1992): 9–12. http://dx.doi.org/10.1042/bj2850009.
Full textAbstract:
Tetanus toxin contains 14 histidine residues: six of them are localized in the light chain (L), one is present in the N-terminal half of the heavy chain (HN) and the remaining seven histidines are localized in the C-terminal half of the heavy chain (Hc). Using immobilized-metal-ion affinity chromatography with Chelating Superose-Zn(II), we show that histidines of Hc are exposed to the protein surface and are responsible for the binding of tetanus toxin and of Hc to the immobilized metal. The histidines of the L chain are not available for co-ordination of matrix-bound Zn2+; however, two of them and three of the histidines of fragment Hc are accessible to diethyl pyrocarbonate. Chromatography on Superose-Zn(II) is also shown to be a simple and efficient method for the rapid isolation of tetanus toxin and of its Hc fragment, which can be extended to the botulinum neurotoxins.
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Heyda, Jan, Philip E. Mason, and Pavel Jungwirth. "Attractive Interactions between Side Chains of Histidine-Histidine and Histidine-Arginine-Based Cationic Dipeptides in Water." Journal of Physical Chemistry B 114, no. 26 (July 8, 2010): 8744–49. http://dx.doi.org/10.1021/jp101031v.
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Doran, John D., and Bruce C. Hill. "Effect of diethyl pyrocarbonate modification on spectral and steady-state kinetic properties of bovine heart cytochrome oxidase." Biochemistry and Cell Biology 70, no. 7 (July 1, 1992): 565–72. http://dx.doi.org/10.1139/o92-087.
Full textAbstract:
The histidine-specific reagent diethyl pyrocarbonate has been used to chemically modify bovine heart cytochrome oxidase. Thirty-two of sixty-seven histidine residues of cytochrome oxidase are accessible to modification by diethyl pyrocarbonate. Effects on the Soret and α bands of the heme spectrum indicate disturbance in the environment of one or both of the heme groups. However, diethyl pyrocarbonate modification does not alter the 830-nm absorbance band, suggesting that the environment of CuA is unchanged. Maximal modification of cytochrome oxidase by diethyl pyrocarbonate results in loss of 85–90% of the steay-state electron transfer activity, which can be reversed by hydroxylamine treatment. However, modification of the first 20 histidines does not alter either activity or the heme spectrum, but only when 32 residues have been modified are the activity and heme spectral changes complete. The steady-state kinetic profile of fully modified oxidase is monophasic; the phase corresponding to tight cytochrome c binding and low turnover is retained, whereas the high turnover phase is abolished. Proteoliposomes incorporated with modified oxidase have a 65% lower respiratory control ratio and 40% lower proton pumping stoichiometry than liposomes containing unmodified oxidase. These results are discussed in terms of a redox-linked proton pumping model for energy coupling via cytochrome oxidase.Key words: cytochrome oxidase, histidine modification, electron transfer, proton pumping, diethyl pyrocarbonate.