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Artykuły w czasopismach na temat „Functional Modeling - Heme Enzymes”

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Data publikacji: 7 września 2023

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1

Timmins, Amy, and Sam P. de Visser. "A Comparative Review on the Catalytic Mechanism of Nonheme Iron Hydroxylases and Halogenases." Catalysts 8, no. 8 (2018): 314. http://dx.doi.org/10.3390/catal8080314.

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Enzymatic halogenation and haloperoxidation are unusual processes in biology; however, a range of halogenases and haloperoxidases exist that are able to transfer an aliphatic or aromatic C–H bond into C–Cl/C–Br. Haloperoxidases utilize hydrogen peroxide, and in a reaction with halides (Cl−/Br−), they react to form hypohalides (OCl−/OBr−) that subsequently react with substrate by halide transfer. There are three types of haloperoxidases, namely the iron-heme, nonheme vanadium, and flavin-dependent haloperoxidases that are reviewed here. In addition, there are the nonheme iron halogenases that s

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2

Robins, Tiina, Jonas Carlsson, Maria Sunnerhagen, Anna Wedell, and Bengt Persson. "Molecular Model of Human CYP21 Based on Mammalian CYP2C5: Structural Features Correlate with Clinical Severity of Mutations Causing Congenital Adrenal Hyperplasia." Molecular Endocrinology 20, no. 11 (2006): 2946–64. http://dx.doi.org/10.1210/me.2006-0172.

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Abstract Enhanced understanding of structure-function relationships of human 21-hydroxylase, CYP21, is required to better understand the molecular causes of congenital adrenal hyperplasia. To this end, a structural model of human CYP21 was calculated based on the crystal structure of rabbit CYP2C5. All but two known allelic variants of missense type, a total of 60 disease-causing mutations and six normal variants, were analyzed using this model. A structural explanation for the corresponding phenotype was found for all but two mutants for which available clinical data are also discrepant with

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Krone, Nils, Yulia Grischuk, Marina Müller, et al. "Analyzing the Functional and Structural Consequences of Two Point Mutations (P94L and A368D) in the CYP11B1 Gene Causing Congenital Adrenal Hyperplasia Resulting from 11-Hydroxylase Deficiency." Journal of Clinical Endocrinology & Metabolism 91, no. 7 (2006): 2682–88. http://dx.doi.org/10.1210/jc.2006-0209.

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Abstract Context: Congenital adrenal hyperplasia is a group of autosomal recessive inherited disorders of steroidogenesis. The deficiency of steroid 11-hydroxylase (CYP11B1) resulting from mutations in the CYP11B1 gene is the second most frequent cause. Objective: We studied the functional and structural consequences of two CYP11B1 missense mutations, which were detected in a 1.8-yr-old boy with acne and precocious pseudopuberty, to prove their clinical relevance and study their impact on CYP11B1 function. Results: The in vitro expression studies in COS-7 cells revealed an almost complete abse

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4

Fontecave, M., S. Ménage, and C. Duboc-Toia. "Functional models of non-heme diiron enzymes." Coordination Chemistry Reviews 178-180 (December 1998): 1555–72. http://dx.doi.org/10.1016/s0010-8545(98)00119-2.

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5

Shteinman, A. A. "Structural-functional modeling of non-heme oxygenases." Russian Chemical Bulletin 60, no. 7 (2011): 1290–300. http://dx.doi.org/10.1007/s11172-011-0197-5.

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6

Yadav, Rahul, and Emily E. Scott. "Endogenous insertion of non-native metalloporphyrins into human membrane cytochrome P450 enzymes." Journal of Biological Chemistry 293, no. 43 (2018): 16623–34. http://dx.doi.org/10.1074/jbc.ra118.005417.

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Human cytochrome P450 enzymes are membrane-bound heme-containing monooxygenases. As is the case for many heme-containing enzymes, substitution of the metal in the center of the heme can be useful for mechanistic and structural studies of P450 enzymes. For many heme proteins, the iron protoporphyrin prosthetic group can be extracted and replaced with protoporphyrin containing another metal, but human membrane P450 enzymes are not stable enough for this approach. The method reported herein was developed to endogenously produce human membrane P450 proteins with a nonnative metal in the heme. This

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7

Nemukhin, A. V., B. L. Grigorenko, I. A. Topol, and S. K. Burt. "Modeling dioxygen binding to the non-heme iron-containing enzymes." International Journal of Quantum Chemistry 106, no. 10 (2006): 2184–90. http://dx.doi.org/10.1002/qua.20910.

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8

Boynton, Tye O., Svetlana Gerdes, Sarah H. Craven, Ellen L. Neidle, John D. Phillips, and Harry A. Dailey. "Discovery of a Gene Involved in a Third Bacterial Protoporphyrinogen Oxidase Activity through Comparative Genomic Analysis and Functional Complementation." Applied and Environmental Microbiology 77, no. 14 (2011): 4795–801. http://dx.doi.org/10.1128/aem.00171-11.

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ABSTRACTTetrapyrroles are ubiquitous molecules in nearly all living organisms. Heme, an iron-containing tetrapyrrole, is widely distributed in nature, including most characterized aerobic and facultative bacteria. A large majority of bacteria that contain heme possess the ability to synthesize it. Despite this capability and the fact that the biosynthetic pathway has been well studied, enzymes catalyzing at least three steps have remained “missing” in many bacteria. In the current work, we have employed comparative genomics via the SEED genomic platform, coupled with experimental verification

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9

Kojima, T., T. Amano, Y. Ishii, and Y. Matsuda. "Ruthenium-pyridylamine complexes as functional models of non-heme iron enzymes." Journal of Inorganic Biochemistry 67, no. 1-4 (1997): 238. http://dx.doi.org/10.1016/s0162-0134(97)80111-0.

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10

Matsunaga, Isamu, and Yoshitsugu Shiro. "Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes." Current Opinion in Chemical Biology 8, no. 2 (2004): 127–32. http://dx.doi.org/10.1016/j.cbpa.2004.01.001.

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11

Atteia, Ariane, Robert van Lis, and Samuel I. Beale. "Enzymes of the Heme Biosynthetic Pathway in the Nonphotosynthetic Alga Polytomella sp." Eukaryotic Cell 4, no. 12 (2005): 2087–97. http://dx.doi.org/10.1128/ec.4.12.2087-2097.2005.

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ABSTRACT Heme biosynthesis involves a number of enzymatic steps which in eukaryotes take place in different cell compartments. Enzyme compartmentalization differs between photosynthetic and nonphotosynthetic eukaryotes. Here we investigated the structures and subcellular localizations of three enzymes involved in the heme pathway in Polytomella sp., a colorless alga evolutionarily related to the green alga Chlamydomonas reinhardtii. Functional complementation of Escherichia coli mutant strains was used to isolate cDNAs encoding three heme biosynthetic enzymes, glutamate-1-semialdehyde aminotra

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12

Park, Hyunchang, and Dongwhan Lee. "Ligand Taxonomy for Bioinorganic Modeling of Dioxygen‐Activating Non‐Heme Iron Enzymes." Chemistry – A European Journal 26, no. 27 (2020): 5916–26. http://dx.doi.org/10.1002/chem.201904975.

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13

Shiro, Yoshitsugu. "Functional Studies on Hemoproteins and Heme-enzymes Based on Their Molecular Structures." Bulletin of Japan Society of Coordination Chemistry 75 (May 31, 2020): 51–56. http://dx.doi.org/10.4019/bjscc.75.51.

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14

Belsare, Ketaki D., Anna Joëlle Ruff, Ronny Martinez, and Ulrich Schwaneberg. "Insights on intermolecular FMN-heme domain interaction and the role of linker length in cytochrome P450cin fusion proteins." Biological Chemistry 401, no. 11 (2020): 1249–55. http://dx.doi.org/10.1515/hsz-2020-0134.

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AbstractCytochrome P450s are an important group of enzymes catalyzing hydroxylation, and epoxidations reactions. In this work we describe the characterization of the CinA–CinC fusion enzyme system of a previously reported P450 using genetically fused heme (CinA) and FMN (CinC) enzyme domains from Citrobacter braaki. We observed that mixing individually inactivated heme (-) with FMN (-) domain in the CinA-10aa linker - CinC fusion constructs results in recovered activity and the formation of (2S)-2β-hydroxy,1,8-cineole (174 µM), a similar amount when compared to the fully functional fusion prot

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15

Mirts, Evan N., Igor D. Petrik, Parisa Hosseinzadeh, Mark J. Nilges, and Yi Lu. "A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme." Science 361, no. 6407 (2018): 1098–101. http://dx.doi.org/10.1126/science.aat8474.

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Multielectron redox reactions often require multicofactor metalloenzymes to facilitate coupled electron and proton movement, but it is challenging to design artificial enzymes to catalyze these important reactions, owing to their structural and functional complexity. We report a designed heteronuclear heme-[4Fe-4S] cofactor in cytochromecperoxidase as a structural and functional model of the enzyme sulfite reductase. The initial model exhibits spectroscopic and ligand-binding properties of the native enzyme, and sulfite reduction activity was improved—through rational tuning of the secondary s

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16

Ha, Edward H., Raymond Y. N. Ho, James F. Kisiel, and Joan Selverstone Valentine. "Modeling the Reactivity of .alpha.-Ketoglutarate-Dependent Non-Heme Iron(II)-Containing Enzymes." Inorganic Chemistry 34, no. 9 (1995): 2265–66. http://dx.doi.org/10.1021/ic00113a002.

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17

Mohammadi, Mahnaz, Fatematossadat Pourseyed Aghaei, Banafsheh Noori, and Esmaeil Pakizeh. "Density Functional Theory modeling of the magnetic susceptibility of heme derivatives." Chemical Physics 527 (November 2019): 110498. http://dx.doi.org/10.1016/j.chemphys.2019.110498.

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18

Badawy, Abdulla A.-B. "Kynurenine Pathway of Tryptophan Metabolism: Regulatory and Functional Aspects." International Journal of Tryptophan Research 10 (January 1, 2017): 117864691769193. http://dx.doi.org/10.1177/1178646917691938.

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Regulatory and functional aspects of the kynurenine (K) pathway (KP) of tryptophan (Trp) degradation are reviewed. The KP accounts for ~95% of dietary Trp degradation, of which 90% is attributed to the hepatic KP. During immune activation, the minor extrahepatic KP plays a more active role. The KP is rate-limited by its first enzyme, Trp 2,3-dioxygenase (TDO), in liver and indoleamine 2,3-dioxygenase (IDO) elsewhere. TDO is regulated by glucocorticoid induction, substrate activation and stabilization by Trp, cofactor activation by heme, and end-product inhibition by reduced nicotinamide adenin

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19

LaBella, Frank S. "Cytochrome P450 enzymes: ubiquitous "receptors" for drugs." Canadian Journal of Physiology and Pharmacology 69, no. 8 (1991): 1129–32. http://dx.doi.org/10.1139/y91-165.

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Most foreign compounds bind to one or more cytochrome P450 drug-metabolizing isozymes. These heme monooxygenases are most concentrated in the endoplasmic reticulum of liver cells but are present in virtually all biological membranes and in all cells. Some radioligands for known hormone receptors have been found to label, with comparable affinities, specific P450 enzymes. A characteristic feature of P450 enzymes is their broad and overlapping drug specificities, with affinity constants ranging over several orders of magnitude. Because fatty acid derivatives and steroids are endogenous substrate

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20

Carrasco, Maria C., and Shabnam Hematian. "(Hydr)oxo-bridged heme complexes: From structure to reactivity." Journal of Porphyrins and Phthalocyanines 23, no. 11n12 (2019): 1286–307. http://dx.doi.org/10.1142/s1088424619300258.

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Iron–porphyrins ([Formula: see text] hemes) are present throughout the biosphere and perform a wide range of functions, particularly those that involve complex multiple-electron redox processes. Some common heme enzymes involved in these processes include cytochrome P450, heme/copper oxidase or heme/non-heme diiron nitric oxide reductase. Consequently, the (hydr)oxo-bridged heme species have been studied for the important roles that they play in many life processes or for their application for catalysis and preparation of new functional materials. This review encompasses important synthetic, s

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21

Arnhold, Jürgen, and Ernst Malle. "Halogenation Activity of Mammalian Heme Peroxidases." Antioxidants 11, no. 5 (2022): 890. http://dx.doi.org/10.3390/antiox11050890.

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Mammalian heme peroxidases are fascinating due to their unique peculiarity of oxidizing (pseudo)halides under physiologically relevant conditions. These proteins are able either to incorporate oxidized halides into substrates adjacent to the active site or to generate different oxidized (pseudo)halogenated species, which can take part in multiple (pseudo)halogenation and oxidation reactions with cell and tissue constituents. The present article reviews basic biochemical and redox mechanisms of (pseudo)halogenation activity as well as the physiological role of heme peroxidases. Thyroid peroxida

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22

Kellmann, Ralf, Toby Mills, and Brett A. Neilan. "Functional Modeling and Phylogenetic Distribution of Putative Cylindrospermopsin Biosynthesis Enzymes." Journal of Molecular Evolution 62, no. 3 (2006): 267–80. http://dx.doi.org/10.1007/s00239-005-0030-6.

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23

Chance, M., L. Powers, C. Kumar, and B. Chance. "X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes." Biochemistry 25, no. 6 (1986): 1259–65. http://dx.doi.org/10.1021/bi00354a010.

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24

Savino, Maria, Claudio Carmine Guida, Maria Nardella, et al. "Circadian Genes Expression Patterns in Disorders Due to Enzyme Deficiencies in the Heme Biosynthetic Pathway." Biomedicines 10, no. 12 (2022): 3198. http://dx.doi.org/10.3390/biomedicines10123198.

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Heme is a member of the porphyrins family of cyclic tetrapyrroles and influences various cell processes and signalling pathways. Enzyme deficiencies in the heme biosynthetic pathway provoke rare human inherited metabolic diseases called porphyrias. Protein levels and activity of enzymes involved in the heme biosynthetic pathway and especially 5′-Aminolevulinate Synthase 1 are featured by 24-h rhythmic oscillations driven by the biological clock. Heme biosynthesis and circadian pathways intermingle with mutual modulatory roles. Notably, heme is a ligand of important cogs of the molecular clockw

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25

Kitanishi, Kenichi, Kazuo Kobayashi, Takeshi Uchida, Koichiro Ishimori, Jotaro Igarashi, and Toru Shimizu. "Identification and Functional and Spectral Characterization of a Globin-coupled Histidine Kinase from Anaeromyxobacter sp. Fw109-5." Journal of Biological Chemistry 286, no. 41 (2011): 35522–34. http://dx.doi.org/10.1074/jbc.m111.274811.

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Two-component signal transduction systems regulate numerous important physiological functions in bacteria. In this study we have identified, cloned, overexpressed, and characterized a dimeric full-length heme-bound (heme:protein, 1:1 stoichiometry) globin-coupled histidine kinase (AfGcHK) from Anaeromyxobacter sp. strain Fw109-5 for the first time. The Fe(III), Fe(II)-O2, and Fe(II)-CO complexes of the protein displayed autophosphorylation activity, whereas the Fe(II) complex had no significant activity. A H99A mutant lost heme binding ability, suggesting that this residue is the heme proximal

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26

Konduri, Purna Chaitanya, Tianyuan Wang, Narges Salamat, and Li Zhang. "Heme, A Metabolic Sensor, Directly Regulates the Activity of the KDM4 Histone Demethylase Family and Their Interactions with Partner Proteins." Cells 9, no. 3 (2020): 773. http://dx.doi.org/10.3390/cells9030773.

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The KDM4 histone demethylase subfamily is constituted of yeast JmjC domain-containing proteins, such as Gis1, and human Gis1 orthologues, such as KDM4A/B/C. KDM4 proteins have important functions in regulating chromatin structure and gene expression in response to metabolic and nutritional stimuli. Heme acts as a versatile signaling molecule to regulate important cellular functions in diverse organisms ranging from bacteria to humans. Here, using purified KDM4 proteins containing the JmjN/C domain, we showed that heme stimulates the histone demethylase activity of the JmjN/C domains of KDM4A a

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27

Hagadorn, John R., Lawrence Que, and William B. Tolman. "A Bulky Benzoate Ligand for Modeling the Carboxylate-Rich Active Sites of Non-Heme Diiron Enzymes." Journal of the American Chemical Society 120, no. 51 (1998): 13531–32. http://dx.doi.org/10.1021/ja983333t.

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Babandi, Abba, Chioma A. Anosike, Lawrence U. S. Ezeanyika, Kemal Yelekçi, and Abdullahi Ibrahim Uba. "Molecular modeling studies of some phytoligands from Ficus sycomorus fraction as potential inhibitors of cytochrome CYP6P3 enzyme of Anopheles coluzzii." Jordan Journal of Pharmaceutical Sciences 15, no. 2 (2022): 258–75. http://dx.doi.org/10.35516/jjps.v15i2.324.

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The major obstacle in controlling malaria is the mosquito’s resistance to insecticides, including pyrethroids. The resistance is mainly due to the over-expression of detoxification enzymes such as cytochromes. Insecticides tolerance can be reduced by inhibitors of P450s involved in insecticide detoxification. Here, to design potential CYP6P3 inhibitors, a homology model of the enzyme was constructed using the crystal structure of retinoic acid-bound cyanobacterial CYP120A1 (PDB ID: 2VE3; Resolution: 2.1 Å). Molecular docking study and computational modeling were employed to determine the inhib

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29

Park, Kiyoung, and Edward I. Solomon. "Modeling nuclear resonance vibrational spectroscopic data of binuclear nonheme iron enzymes using density functional theory." Canadian Journal of Chemistry 92, no. 10 (2014): 975–78. http://dx.doi.org/10.1139/cjc-2014-0067.

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Nuclear resonance vibrational spectroscopy (NRVS) is a powerful technique that can provide geometric structural information on key reaction intermediates of Fe-containing systems when utilized in combination with density functional theory (DFT). However, in the case of binuclear nonheme iron enzymes, DFT-predicted NRVS spectra have been found to be sensitive to the truncation method used to model the active sites of the enzymes. Therefore, in this study various-level truncation schemes have been tested to predict the NRVS spectrum of a binuclear nonheme iron enzyme, and a reasonably sized DFT

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30

Siletsky, Sergey A., and Vitaliy B. Borisov. "Proton Pumping and Non-Pumping Terminal Respiratory Oxidases: Active Sites Intermediates of These Molecular Machines and Their Derivatives." International Journal of Molecular Sciences 22, no. 19 (2021): 10852. http://dx.doi.org/10.3390/ijms221910852.

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Terminal respiratory oxidases are highly efficient molecular machines. These most important bioenergetic membrane enzymes transform the energy of chemical bonds released during the transfer of electrons along the respiratory chains of eukaryotes and prokaryotes from cytochromes or quinols to molecular oxygen into a transmembrane proton gradient. They participate in regulatory cascades and physiological anti-stress reactions in multicellular organisms. They also allow microorganisms to adapt to low-oxygen conditions, survive in chemically aggressive environments and acquire antibiotic resistanc

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31

Naruta, Yoshinori, Masa-aki Sasayama, and Kanako Ichihara. "Functional modeling of managanese-containing O2 evolution enzymes with managanese porphyrin dimers." Journal of Molecular Catalysis A: Chemical 117, no. 1-3 (1997): 115–21. http://dx.doi.org/10.1016/s1381-1169(96)00416-5.

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Majumdar, Amit, and Sabyasachi Sarkar. "Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach." Coordination Chemistry Reviews 255, no. 9-10 (2011): 1039–54. http://dx.doi.org/10.1016/j.ccr.2010.11.027.

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Wan, Dun, Li Fu Liao, and Ying Wu Lin. "Impacts of Uranyl Ion on the Structure and Function of Cytochrome b₅ His39Ser Mutant." Advanced Materials Research 455-456 (January 2012): 1204–9. http://dx.doi.org/10.4028/www.scientific.net/amr.455-456.1204.

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Uranium is toxic to human body with mechanisms not fully understood. The structural and functional consequences of uranyl ions (UO22+) interacting with an axial mutant of cytochrome b5, His39Ser (cyt b5 H39S), were investigated by both spectroscopic and molecular modeling methods. Although slightly disturbs protein folding, UO22+ binding to cyt b5 H39S leads to a decrease of peroxidase activity. A uranyl binding site was further proposed in the heme-binding domain at Glu37 and Glu43. The impacts of UO22+ binding to cyt b5 H39S studied herein provide valuable insights into the toxicity mechanis

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Shumyantseva, Victoria V., Polina I. Koroleva, Tatiana V. Bulko, and Lyubov E. Agafonova. "Alternative Electron Sources for Cytochrome P450s Catalytic Cycle: Biosensing and Biosynthetic Application." Processes 11, no. 6 (2023): 1801. http://dx.doi.org/10.3390/pr11061801.

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The functional significance of cytochrome P450s (CYP) enzymes is their ability to catalyze the biotransformation of xenobiotics and endogenous compounds. P450 enzymes catalyze regio- and stereoselective oxidations of C-C and C-H bonds in the presence of oxygen as a cosubstrate. Initiation of cytochrome P450 catalytic cycle needs an electron donor (NADPH, NADH cofactor) in nature or alternative artificial electron donors such as electrodes, peroxides, photo reduction, and construction of enzymatic “galvanic couple”. In our review paper, we described alternative “handmade” electron sources to su

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35

Tewari, Rajesh Kumar. "Nitric Oxide-Mediated Modulation of Functional Iron Status in Iron-Deficient Maize Plants." INTERNATIONAL JOURNAL OF PLANT AND ENVIRONMENT 5, no. 02 (2019): 78–83. http://dx.doi.org/10.18811/ijpen.v5i02.2.

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Nitric oxide is reported to alleviate Fe-deficiency effects, possibly by enhancing the functional Fe status of plants. Study describes changes in leaf tissue Fe status and consequent modulation of oxidative stress and antioxidant defense in Fe-deficient maize (Zea mays L.) plants supplied with NO. Supply of sodium nitroprusside (SNP), but not of sodium ferrocyanide (SF), caused regreening of leaves, syntheses of chlorophylls and carotenoids and increased activities of hydrogen peroxide-scavenging heme-Fe enzymes and lipid peroxidation, decreased SOD activity and hydrogen peroxide concentration

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Rondelli, Catherine, Aiden Danoff, Hector Bergonia, et al. "Regulation of Erythroid Heme Synthesis By the Mitochondrial Clpx Unfoldase." Blood 134, Supplement_1 (2019): 427. http://dx.doi.org/10.1182/blood-2019-132039.

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Differentiating erythroid cells synthesize large quantities of heme for hemoglobinization. While the transcriptional regulation and enzymatic mechanisms of the heme synthetic enzymes are well characterized, we lack mechanistic understanding of how their protein stability, cofactor incorporation and functional interactions with mitochondrial housekeeping proteins are regulated. These mechanisms can rapidly alter the rate of heme synthesis in response to external stimuli and metabolic requirements, and are critical for heme regulation within a tissue-specific and developmental context. CLPX, a m

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Bela, Krisztina, Riyazuddin Riyazuddin, and Jolán Csiszár. "Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling." Antioxidants 11, no. 8 (2022): 1624. http://dx.doi.org/10.3390/antiox11081624.

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Glutathione peroxidases (GPXs) are non-heme peroxidases catalyzing the reduction of H2O2 or organic hydroperoxides to water or corresponding alcohols using glutathione (GSH) or thioredoxin (TRX) as a reducing agent. In contrast to animal GPXs, the plant enzymes are non-seleno monomeric proteins that generally utilize TRX more effectively than GSH but can be a putative link between the two main redox systems. Because of the substantial differences compared to non-plant GPXs, use of the GPX-like (GPXL) name was suggested for Arabidopsis enzymes. GPX(L)s not only can protect cells from stress-ind

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Acerbi, Enzo, Marcela Hortova-Kohoutkova, Tsokyi Choera, et al. "Modeling Approaches Reveal New Regulatory Networks in Aspergillus fumigatus Metabolism." Journal of Fungi 6, no. 3 (2020): 108. http://dx.doi.org/10.3390/jof6030108.

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Systems biology approaches are extensively used to model and reverse-engineer gene regulatory networks from experimental data. Indoleamine 2,3-dioxygenases (IDOs)—belonging in the heme dioxygenase family—degrade l-tryptophan to kynurenines. These enzymes are also responsible for the de novo synthesis of nicotinamide adenine dinucleotide (NAD+). As such, they are expressed by a variety of species, including fungi. Interestingly, Aspergillus may degrade l-tryptophan not only via IDO but also via alternative pathways. Deciphering the molecular interactions regulating tryptophan metabolism is part

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Satarug, Soisungwan, David A. Vesey, and Glenda C. Gobe. "Mitigation of Cadmium Toxicity through Modulation of the Frontline Cellular Stress Response." Stresses 2, no. 3 (2022): 355–72. http://dx.doi.org/10.3390/stresses2030025.

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Cadmium (Cd) is an environmental toxicant of public health significance worldwide. Diet is the main Cd exposure source in the non-occupationally exposed and non-smoking populations. Metal transporters for iron (Fe), zinc (Zn), calcium (Ca), and manganese (Mn) are involved in the assimilation and distribution of Cd to cells throughout the body. Due to an extremely slow elimination rate, most Cd is retained by cells, where it exerts toxicity through its interaction with sulfur-containing ligands, notably the thiol (-SH) functional group of cysteine, glutathione, and many Zn-dependent enzymes and

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Rovaletti, Anna, Luca De Gioia, Piercarlo Fantucci, et al. "Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes." International Journal of Molecular Sciences 24, no. 7 (2023): 6368. http://dx.doi.org/10.3390/ijms24076368.

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Molecular modeling techniques have become indispensable in many fields of molecular sciences in which the details related to mechanisms and reactivity need to be studied at an atomistic level. This review article provides a collection of computational modeling works on a topic of enormous interest and urgent relevance: the properties of metalloenzymes involved in the degradation and valorization of natural biopolymers and synthetic plastics on the basis of both circular biofuel production and bioremediation strategies. In particular, we will focus on lytic polysaccharide monooxygenase, laccase

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Barreiro, Esther, Alain S. Comtois, Shawn Mohammed, Larry C. Lands, and Sabah N. A. Hussain. "Role of heme oxygenases in sepsis-induced diaphragmatic contractile dysfunction and oxidative stress." American Journal of Physiology-Lung Cellular and Molecular Physiology 283, no. 2 (2002): L476—L484. http://dx.doi.org/10.1152/ajplung.00495.2001.

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Heme oxygenases (HOs), essential enzymes for heme metabolism, play an important role in the defense against oxidative stress. In this study, we evaluated the expression and functional significance of HO-1 and HO-2 in the ventilatory muscles of normal rats and rats injected with bacterial lipopolysaccharide (LPS). Both HO-1 and HO-2 proteins were detected inside ventilatory and limb muscle fibers of normal rats. Diaphragmatic HO-1 and HO-2 expressions rose significantly within 1 and 12 h of LPS injection, respectively. Inhibition of the activity of inducible nitric oxide synthase (iNOS) in rats

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Kim, In Jung, Yannik Brack, Thomas Bayer та Uwe T. Bornscheuer. "Two novel cyanobacterial α-dioxygenases for the biosynthesis of fatty aldehydes". Applied Microbiology and Biotechnology 106, № 1 (2021): 197–210. http://dx.doi.org/10.1007/s00253-021-11724-x.

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Abstractα-Dioxygenases (α-DOXs) are known as plant enzymes involved in the α-oxidation of fatty acids through which fatty aldehydes, with a high commercial value as flavor and fragrance compounds, are synthesized as products. Currently, little is known about α-DOXs from non-plant organisms. The phylogenic analysis reported here identified a substantial number of α-DOX enzymes across various taxa. Here, we report the functional characterization and Escherichia coli whole-cell application of two novel α-DOXs identified from cyanobacteria: CalDOX from Calothrix parietina and LepDOX from Leptolyng

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Empel, Claire, Sripati Jana, and Rene M. Koenigs. "C-H Functionalization via Iron-Catalyzed Carbene-Transfer Reactions." Molecules 25, no. 4 (2020): 880. http://dx.doi.org/10.3390/molecules25040880.

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The direct C-H functionalization reaction is one of the most efficient strategies by which to introduce new functional groups into small organic molecules. Over time, iron complexes have emerged as versatile catalysts for carbine-transfer reactions with diazoalkanes under mild and sustainable reaction conditions. In this review, we discuss the advances that have been made using iron catalysts to perform C-H functionalization reactions with diazoalkanes. We give an overview of early examples employing stoichiometric iron carbene complexes and continue with recent advances in the C-H functionali

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Clark, RA, and N. Borregaard. "Neutrophils autoinactivate secretory products by myeloperoxidase- catalyzed oxidation." Blood 65, no. 2 (1985): 375–81. http://dx.doi.org/10.1182/blood.v65.2.375.375.

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Abstract The neutrophil response to inflammatory stimuli involves the formation of reactive oxygen species and secretion of granule enzymes. In studying secretion of vitamin B12 binding protein by human neutrophils, we noted a major decrease in total recoverable activity from the extracellular fluid plus the stimulated cells (54% of resting cells). Recovery of B12 binding protein from neutrophils exposed to phorbol myristate acetate or opsonized zymosan was significantly enhanced on addition of heme enzyme inhibitors (azide, cyanide) or catalase or when halide-free medium was used. The changes

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Clark, RA, and N. Borregaard. "Neutrophils autoinactivate secretory products by myeloperoxidase- catalyzed oxidation." Blood 65, no. 2 (1985): 375–81. http://dx.doi.org/10.1182/blood.v65.2.375.bloodjournal652375.

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The neutrophil response to inflammatory stimuli involves the formation of reactive oxygen species and secretion of granule enzymes. In studying secretion of vitamin B12 binding protein by human neutrophils, we noted a major decrease in total recoverable activity from the extracellular fluid plus the stimulated cells (54% of resting cells). Recovery of B12 binding protein from neutrophils exposed to phorbol myristate acetate or opsonized zymosan was significantly enhanced on addition of heme enzyme inhibitors (azide, cyanide) or catalase or when halide-free medium was used. The changes in B12 b

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Yudenfreund Kravitz, Joslyn, and Vincent L. Pecoraro. "Synthetic and computational modeling of the vanadium-dependent haloperoxidases." Pure and Applied Chemistry 77, no. 9 (2005): 1595–605. http://dx.doi.org/10.1351/pac200577091595.

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Vanadium-dependent haloperoxidases that catalyze the halogenation of organic substrates using hydrogen peroxide to oxidize halides are a rare class of enzymes which have an absolute requirement for vanadium. In this article, we describe studies using synthetic, small-molecule analogs of the vanadium(V) active site to functionally mimic the oxidation of bromide and thioethers. In addition, we describe computational studies using density functional theory that help describe the mechanism of catalysis.

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Bruijnincx, Pieter C. A., Gerard van Koten, and Robertus J. M. Klein Gebbink. "Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent developments in enzymology and modeling studies." Chemical Society Reviews 37, no. 12 (2008): 2716. http://dx.doi.org/10.1039/b707179p.

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Lee, Dongwhan, and Stephen J. Lippard. "Structural and Functional Models of the Dioxygen-Activating Centers of Non-Heme Diiron Enzymes Ribonucleotide Reductase and Soluble Methane Monooxygenase." Journal of the American Chemical Society 120, no. 46 (1998): 12153–54. http://dx.doi.org/10.1021/ja9831094.

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Rodrigues, Carolina F., Patrícia T. Borges, Magali F. Scocozza, et al. "Loops around the Heme Pocket Have a Critical Role in the Function and Stability of BsDyP from Bacillus subtilis." International Journal of Molecular Sciences 22, no. 19 (2021): 10862. http://dx.doi.org/10.3390/ijms221910862.

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Bacillus subtilis BsDyP belongs to class I of the dye-decolorizing peroxidase (DyP) family of enzymes and is an interesting biocatalyst due to its high redox potential, broad substrate spectrum and thermostability. This work reports the optimization of BsDyP using directed evolution for improved oxidation of 2,6-dimethoxyphenol, a model lignin-derived phenolic. After three rounds of evolution, one variant was identified displaying 7-fold higher catalytic rates and higher production yields as compared to the wild-type enzyme. The analysis of X-ray structures of the wild type and the evolved var

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Dhar, Manoj Kumar, Sonal Mishra, Archana Bhat, Sudha Chib, and Sanjana Kaul. "Plant carotenoid cleavage oxygenases: structure–function relationships and role in development and metabolism." Briefings in Functional Genomics 19, no. 1 (2019): 1–9. http://dx.doi.org/10.1093/bfgp/elz037.

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Abstract A plant communicates within itself and with the outside world by deploying an array of agents that include several attractants by virtue of their color and smell. In this category, the contribution of ‘carotenoids and apocarotenoids’ is very significant. Apocarotenoids, the carotenoid-derived compounds, show wide representation among organisms. Their biosynthesis occurs by oxidative cleavage of carotenoids, a high-value reaction, mediated by carotenoid cleavage oxygenases or carotenoid cleavage dioxygenases (CCDs)—a family of non-heme iron enzymes. Structurally, this protein family di

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