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Academic literature on the topic 'Cytochrom b'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 April 2022

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Journal articles on the topic "Cytochrom b"

1

Ortega, José María, Manuel Hervás, and Manuel Losada. "Isolation and Comparison of Molecular Properties of Cytochrome £-559 from Both Spinach Thylakoids and PS II Particles." Zeitschrift für Naturforschung C 44, no. 5-6 (June 1, 1989): 415–22. http://dx.doi.org/10.1515/znc-1989-5-613.

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Abstract Cytochrome b-559. Spinach Thylakoids. PS II Particles. High and Low Potential. Interconvertible Forms Cytochrome b-559 has been purified from both spinach (Spinacia oleracea L.) thylakoids and photosystem II particles in order to compare some of its more polemic molecular properties. In the two cases, cytochrome 6-559 (which is initially present in its reduced high-potential form and in its oxidized low-potential form) is purified as a single species by preparative disc electrophoresis in Triton-containing polyacrylamide gel, the isolated protein exhibiting similar molecular mass and almost identical low midpoint redox potential and absorption spectra. Moreover, sodium dodecyl sulfate polyacrylamide gel electrophoresis of the purified cytochrom e b-559 reveals, again in both cases, only one polypeptide band of similar molecular mass. Integration o f the isolated low-potential form into liposomes partly restores the high-potential form. These data corroborate our previous results and indicate that there exists in thylakoids only a cytochrome b -559 molecular species tightly bound to PS II and that the two naturally occurring low-and high-potential couples are physiological and correspond to interconvertible states of the genuine hem e protein.

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Besch, Dorothea, Bernd Wissinger, Eberhardt Zrenner, and Beate Leo-Kotter. "Ein Fall von Leberscher Optikusneuropathie (LHON) mit einer neuen Punktmutation im Cytochrom-b-Gen." Der Ophthalmologe 97, no. 1 (January 27, 2000): 27–32. http://dx.doi.org/10.1007/pl00007105.

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Szczepaniak, A., M. T. Black, and W. A. Cramer. "Topography of the Chloroplast Cytochrome b6: Orientation of the Cytochrome and Accessibility of the Lumen-Side Interhelix Loops." Zeitschrift für Naturforschung C 44, no. 5-6 (June 1, 1989): 453–61. http://dx.doi.org/10.1515/znc-1989-5-619.

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Abstract The to pography of chloroplast cytochromes f and b6 was probed with proteases carboxypeptidase A (CpA ), trypsin, and Staph, aureus V8. The cytochrome and its proteolytic products were detected by heme stain and, in most experiments, by immunoreaction. In thylakoids, the only protease that significantly affected the intactness of cytochrome f was CpA that caused a small (ΔMr = -1 - 2000) decrease in the apparent molecular weight. In SDS -treated thylakoids, both trypsin and V8 degraded cytochrome f. The inferred topography of cytochrom f , with the COOH -terminus on the stromal (n) side, one membrane-spanning a-helix n ear the COOH-terminus, and most of the Cyt f mass on the lumen (p) side, is consistent with that previously inferred by others. Cytochrome b6 was not sensitive to CpA . but was more sensitive to trypsin and V8 protease than cytochrome f , cytochrome b-559, or the 17 kDa OEC extrinsic protein. Trypsin caused a small decrease in size of cytochrome b6, which was observed using whole protein antibody as a single smaller band (ΔMr ≈ 2000) or two smaller discrete bands (ΔMr = -1000 and 2500, respectively) which, unlike the untreated protein , did not react with antibody generated to a peptide mimicking A sp-5 -Gln-14 near the NH2-terminus. These shorten ed tryptic fragments were attributed to cleavage after R-10 and K-23 n ear the NH2-terminus, implying an orientation with the NH2-terminus on the stromal side of the membrane. The sensitivity of cytochrome b6 toward this trypsin cleavage was increased if the membranes were first incubated with CpA , showing that the NH2 -terminal region of cytochrome b6 is masked by the COOH -terminal domain of one or more thylakoid proteins. Under conditions where degradation of cytochrome b-559, cytochrome f, or the 17 kDa OEC extrinsic protein on the lumen side of the membrane was small ( < 10-20% ). V8 protease degraded 80-90% of cytochrome b6. The main polypeptide fragment generated by V8 protease had an apparent molecular weight Mr = 16,000, reacted with antibody to a peptide mimicking Ala-146-Asp-155, and was more pronounced in membranes treated with SDS. The fragment could then result from cleavage at two sites, Glu-74 and /or Glu-166. It is concluded that the loop of cytochrome b6 protruding from the lumen side of the membrane between helices III and IV , and possibly that between helices I and II as w ell, contains a single Glu residue conferring a sensitivity to V8 protease greater than that of the lumen-side mass of cytochrome f which has many more Glu residues. This implies a lumen-skeletal structure in which one or two loops of cytochrome b6 on the lumen side are more exposed to the aqueous phase than cytochrome f.

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Wiesemann, Frank, Ralf Wonnemann, Bernt Krebs, Heike Keutel, and Ernst-G. Jäger. "Orientierungswechsel axialer Imidazolliganden in einem Cytochrom-b-Modellkomplex in Abhängigkeit von der Oxidationsstufe des Metallzentrums." Angewandte Chemie 106, no. 13 (July 4, 1994): 1424–26. http://dx.doi.org/10.1002/ange.19941061313.

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Zimmermann, Stefanie, R. Zehner, and A. Herzog. "Cytochrom b-Sequenz-Vergleiche zwischen Wisent(Bison bison bonasus) und Hausrind(Bos primigenius f. taurus)." Zeitschrift für Jagdwissenschaft 44, no. 1 (March 1998): 26–32. http://dx.doi.org/10.1007/bf02239881.

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6

Buntin, Kathrin, Shwan Rachid, Maren Scharfe, Helmut Blöcker, Kira J Weissman, and Rolf Müller. "Produktion der Isochromanon-Antimykotika Ajudazol A und B inChondromyces crocatus Cm c5: Biosynthesemaschinerie und Cytochrom-P450-Modifikationen." Angewandte Chemie 120, no. 24 (June 2, 2008): 4671–76. http://dx.doi.org/10.1002/ange.200705569.

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7

Yamada, Mitsunori, Kaoru Nakasone, Hideyuki Tamegai, Chiaki Kato, Ron Usami, and Koki Horikoshi. "Pressure Regulation of Soluble Cytochromesc in a Deep-Sea Piezophilic Bacterium,Shewanella violacea." Journal of Bacteriology 182, no. 10 (May 15, 2000): 2945–52. http://dx.doi.org/10.1128/jb.182.10.2945-2952.2000.

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ABSTRACT Two c-type cytochromes from the soluble fraction of a deep-sea moderately piezophilic bacterium, Shewanella violacea, were purified and characterized, and the genes coding for these cytochromes were cloned and sequenced. One of the cytochromes, designated cytochrome c A, was found to have a molecular mass of approximately 8.3 kDa, and it contained one heme c per molecule. The other, designated cytochrome c B, was found to have a molecular mass of approximately 23 kDa, and it contained two heme cmolecules per protein molecule. The amount of cytochromec B expressed in cells grown at high hydrostatic pressure (50 MPa) was less than that in cells grown at atmospheric pressure, whereas cytochrome c A was constitutively expressed under all pressure conditions examined. The results of Northern blotting analysis were consistent with the above-mentioned observations and suggested that the pressure regulation of cytochrome c B gene expression occurred at the transcriptional level. These results suggest that the components of the respiratory chain of moderately piezophilic S. violaceacould be exchanged according to the growth pressure conditions.

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Stüber, Frank, and Ulrike Stamer. "Pharmakogenetik und pädiatrische Schmerztherapie." Kinder- und Jugendmedizin 4, no. 05 (2004): 161–67. http://dx.doi.org/10.1055/s-0037-1617830.

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ZusammenfassungNeue Erkenntnisse über die Struktur des Genoms und die Entdeckung genomischer Varianten haben die genetische Diagnostik sowohl für komplexe und akute Erkrankungen als auch für den Bereich Pharmakogenetik interessant werden lassen.Für einige Bereiche, z. B. der großen Gruppe der metabolisierenden Enzyme, liegen schon Untersuchungen vor, die zeigen, dass genetische Varianten einen Einfluss auf Effektivität und Nebenwirkungen von Arzneimitteln haben. So erfahren Patienten mit einer Defizienz für das Cytochrom P450-Isoenzym 2D6 keine oder nur eine reduzierte Analgesie durch Codein und Tramadol. Auch für die Wirksamkeit und die Nebenwirkungen von Nichtopioid-Analgetika können genetische Varianten eine Rolle spielen.Erkenntnisse aus dem Bereich der Pharmakogenetik werden es in Zukunft erlauben, die Therapie der individuellen (genetischen) Konstellation anzupassen.

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Saribas, A. Sami, Sevnur Mandaci, and Fevzi Daldal. "An Engineered Cytochromeb6c1 Complex with a Split Cytochrome b Is Able To Support Photosynthetic Growth of Rhodobacter capsulatus." Journal of Bacteriology 181, no. 17 (September 1, 1999): 5365–72. http://dx.doi.org/10.1128/jb.181.17.5365-5372.1999.

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ABSTRACT The ubihydroquinone-cytochrome c oxidoreductase (or the cytochrome bc 1 complex) fromRhodobacter capsulatus is composed of the Fe-S protein, cytochrome b, and cytochromec 1 subunits encoded bypetA(fbcF), petB(fbcB), and petC(fbcC) genes organized as an operon. In the work reported here, petB(fbcB) was split genetically into two cistrons, petB6 andpetBIV, which encoded two polypeptides corresponding to the four amino-terminal and four carboxyl-terminal transmembrane helices of cytochrome b, respectively. These polypeptides resembled the cytochromeb 6 and su IV subunits of chloroplast cytochromeb 6 f complexes, and together with the unmodified subunits of the cytochromebc 1 complex, they formed a novel enzyme, named cytochrome b 6 c 1complex. This membrane-bound multisubunit complex was functional, and despite its smaller amount, it was able to support the photosynthetic growth of R. capsulatus. Upon further mutagenesis, a mutant overproducing it, due to a C-to-T transition at the second base of the second codon of petBIV, was obtained. Biochemical analyses, including electron paramagnetic spectroscopy, with this mutant revealed that the properties of the cytochromeb 6 c 1 complex were similar to those of the cytochrome bc 1 complex. In particular, it was highly sensitive to inhibitors of the cytochrome bc 1 complex, including antimycin A, and the redox properties of its b- and c-type heme prosthetic groups were unchanged. However, the optical absorption spectrum of its cytochrome b L heme was modified in a way reminiscent of that of a cytochromeb 6 f complex. Based on the work described here and that with Rhodobacter sphaeroides (R. Kuras, M. Guergova-Kuras, and A. R. Crofts, Biochemistry 37:16280–16288, 1998), it appears that neither the inhibitor resistance nor the redox potential differences observed between the bacterial (or mitochondrial) cytochromebc 1 complexes and the chloroplast cytochromeb 6 f complexes are direct consequences of splitting cytochrome b into two separate polypeptides. The overall findings also illustrate the possible evolutionary relationships among various cytochrome bcoxidoreductases.

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Buntin, Kathrin, Shwan Rachid, Maren Scharfe, Helmut Blöcker, Kira J Weissman, and Rolf Müller. "Produktion der Isochromanon-Antimykotika Ajudazol A und B in Chondromyces crocatus Cm c5: Biosynthesemaschinerie und Cytochrom-P450-Modifikationen." Angewandte Chemie 121, no. 52 (December 15, 2009): 9957. http://dx.doi.org/10.1002/ange.200990260.

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Dissertations / Theses on the topic "Cytochrom b"

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Tome, Lydia [Verfasser]. "Faltung, Assemblierung und Stabilisierung des Transmembranproteins Cytochrom b 6 / Lydia Tome." Mainz : Universitätsbibliothek Mainz, 2015. http://d-nb.info/1064854745/34.

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Krause-Buchholz, Udo. "Translationsaktivatoren der mitochondrialen Cytochrom b-Synthese in Saccaromyces cerevisiae: Membranassoziation, Mutagenese und Protein-Wechselwirkungen von Cbs1p." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2000. http://nbn-resolving.de/urn:nbn:de:swb:14-991052844578-08818.

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Die vorliegende Arbeit beschäftigt sich mit Cbs1p und Cbs2p, zwei spezifische Translationsaktivatoren der COB-mRNA. Im Mittelpunkt standen sowohl die weitere molekularbiologische und biochemische Charakterisierung von Cbs1p als auch ein Screening von Interaktionskandidaten, die mit Cbs1p und/oder Cbs2p physikalisch wechselwirken könnten. Cbs1p liegt als peripheres Membranprotein fest mit der inneren Mitochondrienmembran matrixseitig assoziiert vor. Dabei spielen möglicherweise hydrophobe und/oder Protein-Protein-Wechselwirkungen mit integralen Membranproteinen eine essentielle Rolle bei der Membranverankerung von Cbs1p. Durch die Identifizierug von atmungsdefekten Cbs1p-Mutanten, deren Mutationen in Bereichen mit Homologie zu RNA-bindenden Proteinen liegt, verstärken sich die Hinweise zur Beteiligung von Cbs1p an der direkten physikalischen Wechselwirkung mit dem 5´-leader der COB-mRNA. Darüber hinaus konnte gezeigt werden,, dass die abspaltbare Präsequenz nicht notwendig für einen mitochondrialen Import ist. Die Ergebnisse präzisieren und erweitern das vorliegende Modell der Wirkungsweise der Translationsaktivatoren Cbs1p und Cbs2p (Michaelis, 1991). Aufgrund der Membranverankerung von Cbs1p wird auch die gebundene COB-mRNA in räumlicher Nähe zur Membran gebracht. Darüber hinaus definiert Cbs1p damit möglicherweise auch den Ort der Insertion des nascierenden Apocytochrom b in die Membran. Cbs2p vermittelt die Bindung zur kleinen Untereinheit der mitochondrialen Ribosomen und könnte seinerseits ebenfalls in Interaktionen mit Untereinheiten des bc1-Komplexes involviert sein.

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Hansmann, Tobias [Verfasser], Ulrike [Akademischer Betreuer] Schmidt, and Jana [Akademischer Betreuer] Naue. "Differenzierung von Spezies durch familienspezifische Amplifikation und HRM-Analyse mitochondrialer Genabschnitte (12S rRNA, Cytochrom b)." Freiburg : Universität, 2017. http://d-nb.info/1151446483/34.

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Kranz-Finger, Sarah [Verfasser], Vlada B. [Gutachter] Urlacher, and Karl-Erich [Gutachter] Jaeger. "Oxidation pflanzlicher Triterpenoide mittels Cytochrom-P450-Monooxygenasen / Sarah Kranz-Finger ; Gutachter: Vlada B. Urlacher, Karl-Erich Jaeger." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2019. http://d-nb.info/1196870691/34.

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Kranz-Finger, Sarah Katharina [Verfasser], Vlada B. [Gutachter] Urlacher, and Karl-Erich [Gutachter] Jaeger. "Oxidation pflanzlicher Triterpenoide mittels Cytochrom-P450-Monooxygenasen / Sarah Kranz-Finger ; Gutachter: Vlada B. Urlacher, Karl-Erich Jaeger." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2019. http://d-nb.info/1196870691/34.

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Le-Huu, Priska [Verfasser], Vlada B. [Akademischer Betreuer] Urlacher, and Martina [Akademischer Betreuer] Pohl. "Cytochrom-P450-Biokatalyse: Selektive Oxidation von 14-gliedrigen Makrozyklen und Diterpenoiden / Priska Le-Huu. Gutachter: Vlada B. Urlacher ; Martina Pohl." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2016. http://d-nb.info/1082033871/34.

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Tapalaga, Dan. "NFkB NF-kappa-B, Caspase 3 und Cytochrom-c-Oxidase Licht- und elektronenmikroskopische, immunhistochemische sowie biochemische Untersuchungen am GalN-TNF-[alpha]-Modell der Maus /." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=967778077.

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Eltis, Lindsay David. "Interaction of cytochrome b₅ and cytochrome c." Thesis, University of British Columbia, 1989. http://hdl.handle.net/2429/29096.

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The interaction and kinetics of electron transfer between cytochrome b₅ and cytochrome c, two well characterised soluble electron transfer proteins, have been investigated by three techniques. First, fluorescence quenching experiments were done with cytochrome b₅ and porphyrin cytochrome c, a fluorescent analogue of cytochrome c. These quenching studies yielded association constants and structural information for the cytochrome b₅ cytochrome c complex. Second, an analysis of the rate of flavin semiquinone reduction of the cytochromes within the cytochrome b₅ cytochrome c complex yielded information about the structure and electrostatics of die complex. Third, the second order rate constant for ferrocytochrome b₅ reduction of ferricytochrome c was determined under a variety of solution conditions by stopped-flow spectroscopy. Particular effort was directed at evaluating the role of the cytochrome bs heme propionates in the interaction and electron transfer between cytochrome b₅ and c through performing each of diese three studies with a derivative of cytochrome b₅ in which die heme propionates had been esterified (referred to as DME-cytochrome b₅). The fluorescence quenching studies on the interaction of cytochrome b₅ and porphyrin cytochrome c and die kinetics of flavin semiquinone reduction of the proteins within the cytochrome b₅ cytochrome c complex provided evidence that esterification of the cytochrome b₅ heme propionates, influences the docking geometry of the two proteins. These findings support the predictions of electrostatic calculations [Mauk, M.R., Mauk, A.G., Weber, P.C. & Matthew, J.B. (1986) Biochemistry, 25, 7085] in two respects. First, esterification of the cytochrome b₅ heme propionates detectably increases the separation between die two heme groups in die cytochrome b₅ cytochrome c complex. Second, die cytochrome c heme group is not as sterically hindered in the DME-cytochiome b₅ cytochrome c complex as in die cytochrome b₅ cytochrome c complex. The stopped-flow studies demonstrate that the bimolecular rate constant for ferrocytochrome b₅ reduction of ferricytochrome c is determined in part by the rate of association of the two proteins. This rate of association is strongly influenced by electrostatic forces. The principal effect of esterification of the cytochrome b₅ heme propionates on the second order rate of electron transfer between cytochromes bs and c is to influence complex formation between these two proteins. The stopped-flow studies further suggest that the reduction potentials of native and DME-cytochromes b₅ are not significantly different when these proteins are bound to cytochrome c. The nature of electron transfer protein-protein interactions and protein-protein electron transfer is discussed with respect to these findings.
Medicine, Faculty of
Biochemistry and Molecular Biology, Department of
Graduate

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Raina, Vikrant. "Part A. Synthesis of Second Generation Dillapiol and Sesamol Analogues; Inhibition of Cytochrom P450 3A4. Part B. Synthesis of Analogs of Z02; Compounds with Potential to Help Regenerate Partially Severed Spinal Cords." Thesis, Université d'Ottawa / University of Ottawa, 2018. http://hdl.handle.net/10393/38462.

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Dillapiol is a naturally occurring methylenedioxyphenyl (MDP) compound that acts as an insecticide synergist comparable in activity to the widely used piperonyl butoxide (PBO). More than thirty synthetic analogs of dillapiol and sesamol were prepared and evaluated for their inhibitory activity in a cloned human Cytochrome P450 3A4 (CYP 3A4) enzyme in order to assess their use as pesticide synergists and to determine the next generation of compounds. These compounds represent a second generation of analogs based on the knowledge gained from compounds prepared and evaluated by a former member of our group. The choice of new structures was also influenced by the surprising and important observations by Dr. Suqi Liu that compound 21 inhibited not only CYP 3A4 but also glutathione-S- transferase (GST). A set of compounds related to 21 were sent to BASF (Durham NC) for evaluation of their synergistic activity, toxicity and persistence in soil studies. In a number of instances these analogs outperformed PBO as synergists even when given at 1:1 synergist: pesticide ratio compared to PBO at 5:1 when tested against a variety of resistant insects in BASF laboratories in the USA, Holland, India and Indonesia. All of the compounds were shown to be non-toxic to animal life. Their half-life in soils was typically less than 10 days. The results obtained form the basis of two BASF - University of Ottawa patent applications. The most potent CYP3A4 inhibitors synthesized as part of this project are the sulfones 15and 15a. These compounds are 107 and 71 times more potent than dillapiol, respectively which has an IC50 of 8.9 ±0.3 µM. The ortho- chlorobenzyl ether 48 was shown to be 74 times more potent than dillapiol. The synthesis of Z02 analogs in which the NH and C (O) substituents of the B unit are in the ortho-, meta- and para-orientation compared to the meta-orientation of Z02 is reported. The bioactivities of these compounds were compared with previously synthesized meta- substituted analogs to determine which of the three orientations, ortho-, meta-, or para-, resulted in the most potent compounds. In vitro bioassay results obtained by the Brown group allow us to draw conclusions on the effects of the structural characteristics necessary for optimization of activity. Results acquired thus far have suggested that both the ortho- or para- substituted analogs have reduced activity relative to the meta- substituted analogs. Replacement of the oxygen in the CD unit by a sulfoxide and sulfone gave compounds with slightly improved inhibition of SOX9 but with still lower activity relative to Z02. The SAR performed in this project did not result in compounds superior to Z02. Nevertheless, the results described in this thesis give guidance for future SAR studies. It is recommended that future synthetic efforts be concentrated on the metaoriented analogs.

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Steinebrunner, Iris, Uta Gey, Manuela Andres, Lucila Garcia, and Daniel H. Gonzalez. "Divergent functions of the Arabidopsis mitochondrial SCO proteins: HCC1 is essential for COX activity while HCC2 is involved in the UV-B stress response." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2014. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-147367.

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The two related putative cytochrome c oxidase (COX) assembly factors HCC1 and HCC2 from Arabidopsis thaliana are Homologs of the yeast Copper Chaperones Sco1p and Sco2p. The hcc1 null mutation was previously shown to be embryo lethal while the disruption of the HCC2 gene function had no obvious effect on plant development, but increased the expression of stress-responsive genes. Both HCC1 and HCC2 contain a thioredoxin domain, but only HCC1 carries a Cu-binding motif also found in Sco1p and Sco2p. In order to investigate the physiological implications suggested by this difference, various hcc1 and hcc2 mutants were generated and analyzed. The lethality of the hcc1 knockout mutation was rescued by complementation with the HCC1 gene under the control of the embryo-specific promoter ABSCISIC ACID INSENSITIVE 3. However, the complemented seedlings did not grow into mature plants, underscoring the general importance of HCC1 for plant growth. The HCC2 homolog was shown to localize to mitochondria like HCC1, yet the function of HCC2 is evidently different, because two hcc2 knockout lines developed normally and exhibited only mild growth suppression compared with the wild type (WT). However, hcc2 knockouts were more sensitive to UV-B treatment than the WT. Complementation of the hcc2 knockout with HCC2 rescued the UV-B-sensitive phenotype. In agreement with this, exposure of wild-type plants to UV-B led to an increase of HCC2 transcripts. In order to corroborate a function of HCC1 and HCC2 in COX biogenesis, COX activity of hcc1 and hcc2 mutants was compared. While the loss of HCC2 function had no significant effect on COX activity, the disruption of one HCC1 gene copy was enough to suppress respiration by more than half compared with the WT. Therefore, we conclude that HCC1 is essential for COX function, most likely by delivering Cu to the catalytic center. HCC2, on the other hand, seems to be involved directly or indirectly in UV-B-stress responses.

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Books on the topic "Cytochrom b"

1

Kiel, Johnathan L. Type-b cytochromes: Sensors and switches. Boca Raton: CRC Press, 1995.

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Lu, Guoguang. Structural studies on nitrate reductase, a nitrogen assimilating enzyme. Uppsala: Dept. of Molecular Biology, Swedish University of Agricultural Sciences, 1994.

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Clarke, Jacqueline. The cytochrome P450 - dependent - minced function oxidases and the functional integrity of the pancreatic B-cell. [S.l: The Author], 1997.

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Cytochromes b and c: Biochemical Properties, Biological Functions and Electrochemical Analysis. Nova Science Pub Inc, 2014.

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Type-B Cytochromes: Sensors and Switches. Taylor & Francis Group, 2017.

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Kiel, Johnathan L. Type-B Cytochromes: Sensors and Switches. CRC Press, 2018. http://dx.doi.org/10.1201/9781351077415.

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Meek, Laura. Hydrogenase in Azotobacter vinelandii: The role of the heme ligands in HoxZ. 1999.

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(Editor), John N. Abelson, Melvin I. Simon (Editor), Eric F. Johnson (Editor), and Michael R. Waterman (Editor), eds. Methods in Enzymology, Volume 272: Cytochrome P450, Part B (Methods in Enzymology,). Academic Press, 1996.

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(Editor), John N. Abelson, Melvin I. Simon (Editor), Eric F. Johnson (Editor), and Michael R. Waterman (Editor), eds. Methods in Enzymology, Volume 272: Cytochrome P450, Part B (Methods in Enzymology,). Academic Press, 1996.

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Fabbri, Chiara, and Alessandro Serretti. The treatment of bipolar disorder in the era of personalized medicine: myth or promise? Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198748625.003.0031.

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Bipolar disorder (BD) is a chronic disease associated with high personal and socio-economic burden. Genetics accounts for 20–95% of variability in central nervous system drug disposition and pharmacodynamics, thus genetic markers are considered a promising way to develop tailored treatments and improve the prognosis of the disease. Among mood stabilizers, lithium response was the most investigated phenotype and the most replicated genes are involved in synaptic plasticity (BDNF), serotonergic (SLC6A4) and dopaminergic (DRD1) neurotransmission, and second messenger cascades (GSK3B). Relevant pharmacogenetic findings regarding other mood stabilizers are hyperammonaemia (CPS1 gene) and hepatic dysfunction (POLG gene) induced by valproate and immune-mediated cutaneous hypersensitivity reactions (HLA-B*1502) induced by lamotrigine or carbamazepine. Polymorphisms in cytochrome (CYP) P450 genes are expected to provide useful information particularly in case of polypharmacy. Despite few pharmacogenetic tests are currently recommended, the development of pharmacogenetics in other fields of medicine provides an encouraging perspective.

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Book chapters on the topic "Cytochrom b"

1

Yu, Chang-An, and Linda Yu. "Mitochondrial Cytochrome b 560." In Cytochrome Systems, 649–56. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_89.

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Howell, Neil, and Karin Gilbert. "Sequence Analysis of Mammalian Cytochrome b Mutants." In Cytochrome Systems, 79–86. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_9.

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Koch, Hans-Georg, and Dirk Schneider. "Assembly of Transmembrane b-Type Cytochromes and Cytochrome Complexes." In Advances in Photosynthesis and Respiration, 555–84. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-017-7481-9_28.

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Boffoli, D., M. Lorusso, and S. Papa. "Effect of Antimycin on the Kinetics of Reduction of b and c1 Cytochromes in Single Turnover of the Mitochondrial b-c1 Complex." In Cytochrome Systems, 669–71. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_91.

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Gabellini, Nadia A. "Structural Homologies in the Cytochrome B/C1 Complex from Rhodobacter." In Cytochrome Systems, 35–40. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_4.

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Pacoda, D., A. S. Treglia, L. Siculella, C. Perrotta, and R. Gallerani. "Localization and Partial Sequencing Analysis of Mitochondrial Gene for Apocytochrome B in Sunflower." In Cytochrome Systems, 133–34. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_16.

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de Vries, S., A. N. van Hoek, A. ten Bookum, and J. A. Berden. "The Kinetics of Oxidation of Cytochrome B are in Agreement with the Q-Cycle Hypothesis." In Cytochrome Systems, 517–22. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_72.

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Barber, J., K. Gounaris, and D. J. Chapman. "Isolation of the Photosystem Two Reaction Centre and the Location and Function of Cytochrome b-559." In Cytochrome Systems, 657–66. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_90.

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West, I. C. "Electron Conduction Between b Cytochromes of the Mitochondrial Respiratory Chain in the Presence of Antimycin Plus Myxothiazol." In Cytochrome Systems, 679–80. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_94.

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Solaini, G., M. Crimi, F. Ballester, M. Degli Esposti, and G. Lenaz. "The Circular Dichroism Properties of the Rieske Protein and the b and c1 Cytochromes of the Mitochondrial bc1 Complex." In Cytochrome Systems, 337–38. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_44.

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Conference papers on the topic "Cytochrom b"

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Tri Widodo, Wimbuh, Abdul Hadi furqoni, Ahmad Yudianto, and Sri Puji Astuti Wahyuningsih. "Identification Human and Animal Blood Mixtures Using Human Cytochrome b Gene." In 1st International Conference Postgraduate School Universitas Airlangga : "Implementation of Climate Change Agreement to Meet Sustainable Development Goals" (ICPSUAS 2017). Paris, France: Atlantis Press, 2018. http://dx.doi.org/10.2991/icpsuas-17.2018.81.

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Ming-cheng, Li, Wang Mao, Liu Tong-hui, Wang Jin, and Zhang Li-hua. "Identification on cytochrome b of Testudinis Carapax et Plastrum and its adulterants." In 2011 International Conference on Human Health and Biomedical Engineering (HHBE). IEEE, 2011. http://dx.doi.org/10.1109/hhbe.2011.6028960.

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Rajkhowa, D., and D. J. Kalita. "Fingerprinting and Sequencing of Mitochondrial Cytochrome B Gene of Cattle, Buffalo and Yak." In Annual International Conference on Advances in Veterinary Science Research. Global Science & Technology Forum (GSTF), 2013. http://dx.doi.org/10.5176/2382-5685_vetsci13.37.

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Holloway, Peter W., and Henry H. Mantsch. "FTIR Analysis Of Cytochrome b s In H 2 O And D 2 O." In Intl Conf on Fourier and Computerized Infrared Spectroscopy, edited by David G. Cameron. SPIE, 1989. http://dx.doi.org/10.1117/12.969453.

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Permana, Deby, Jarulis, Sipriyadi, and Santi Nurul Kamilah. "Genetic Variation of Black Capped White Eye Zosterops atricapilla (Aves: Zosteropidae) Based on Mitochondrial DNA Cytochrome B Gene." In 3rd KOBI Congress, International and National Conferences (KOBICINC 2020). Paris, France: Atlantis Press, 2021. http://dx.doi.org/10.2991/absr.k.210621.058.

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Salamah, Nina, Yuny Erwanto, Sudibyo Martono, and Abdul Rohman. "Porcine-specific Primer based on Cytochrome B by Real-Time Polymerase Chain Reaction Method for Identification in Raw Meat." In Proceedings of the 2019 Ahmad Dahlan International Conference Series on Pharmacy and Health Science (ADICS-PHS 2019). Paris, France: Atlantis Press, 2019. http://dx.doi.org/10.2991/adics-phs-19.2019.29.

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Miao, Wang, Liu Yang, Zhang Li-hua, and Yang Ming-yan. "Characterization and identification of cytochrome b DNA fingerprinting between the penis et testis of the Cervus nippon Temmink and the bullwhip." In 2011 International Conference on Human Health and Biomedical Engineering (HHBE). IEEE, 2011. http://dx.doi.org/10.1109/hhbe.2011.6027966.

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Sipriyadi, Hasriany Vellarenza, and Choirul Muslim. "The Analysis of Pork Content in Processed Beef Meatballs at Ketahun, North Bengkulu District Using Genetic Marker Mitochondrial DNA Cytochrome b." In 3rd KOBI Congress, International and National Conferences (KOBICINC 2020). Paris, France: Atlantis Press, 2021. http://dx.doi.org/10.2991/absr.k.210621.068.

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Nor Farah, S. H., M. Y. Norfatimah, and M. L. Siti Noor Hajjar. "Genetic variation of Mahseer Tor spp. in Pahang National Park using cytochrome b mtDNA gene based on phylogenetic analysis - a research framework." In its Applications (CSPA). IEEE, 2011. http://dx.doi.org/10.1109/cspa.2011.5759846.

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Mohd-Yusof, Nur Syafika, Juliana Senawi, Jeffrine Japning Rovie-Ryan, Shukor Md Nor, and Badrul Munir Md-Zain. "Phylogenetic relationships of Island flying fox, Pteropus hypomelanus (chiroptera: Pteropodidae) along the east and west coast of Peninsular Malaysia based on Cytochrome b sequences." In THE 2018 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2018 Postgraduate Colloquium. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5111278.

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Reports on the topic "Cytochrom b"

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Ohad, Itzhak, and Himadri Pakrasi. Role of Cytochrome B559 in Photoinhibition. United States Department of Agriculture, December 1995. http://dx.doi.org/10.32747/1995.7613031.bard.

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Abstract:

The aim of this research project was to obtain information on the role of the cytochrome b559 in the function of Photosystem-II (PSII) with special emphasis on the light induced photo inactivation of PSII and turnover of the photochemical reaction center II protein subunit RCII-D1. The major goals of this project were: 1) Isolation and sequencing of the Chlamydomonas chloroplast psbE and psbF genes encoding the cytochrome b559 a and b subunits respectively; 2) Generation of site directed mutants and testing the effect of such mutation on the function of PSII under various light conditions; 3) To obtain further information on the mechanism of the light induced degradation and replacement of the PSII core proteins. This information shall serve as a basis for the understanding of the role of the cytochrome b559 in the process of photoinhibition and recovery of photosynthetic activity as well as during low light induced turnover of the D1 protein. Unlike in other organisms in which the psbE and psbF genes encoding the a and b subunits of cytochrome b559, are part of an operon which also includes the psbL and psbJ genes, in Chlamydomonas these genes are transcribed from different regions of the chloroplast chromosome. The charge distribution of the derived amino-acid sequences of psbE and psbF gene products differs from that of the corresponding genes in other organisms as far as the rule of "positive charge in" is concerned relative to the process of the polypeptide insertion in the thylakoid membrane. However, the sum of the charges of both subunits corresponds to the above rule possibly indicating co-insertion of both subunits in the process of cytochrome b559 assembly. A plasmid designed for the introduction of site-specific mutations into the psbF gene of C. reinhardtii. was constructed. The vector consists of a DNA fragment from the chromosome of C. reinhardtii which spans the region of the psbF gene, upstream of which the spectinomycin-resistance-conferring aadA cassette was inserted. This vector was successfully used to transform wild type C. reinhardtii cells. The spectinomycin resistant strain thus obtained can grow autotrophically and does not show significant changes as compared to the wild-type strain in PSII activity. The following mutations have been introduced in the psbF gene: H23M; H23Y; W19L and W19. The replacement of H23 involved in the heme binding to M and Y was meant to permit heme binding but eventually alter some or all of the electron transport properties of the mutated cytochrome. Tryptophane W19, a strictly conserved residue, is proximal to the heme and may interact with the tetrapyrole ring. Therefore its replacement may effect the heme properties. A change to tyrosine may have a lesser affect on the potential or electron transfer rate while a replacement of W19 by leucine is meant to introduce a more prominent disturbance in these parameters. Two of the mutants, FW19L and FH23M have segregated already and are homoplasmic. The rest are still grown under selection conditions until complete segregation will be obtained. All mutants contain assembled and functional PSII exhibiting an increased sensitivity of PSII to the light. Work is still in progress for the detailed characterization of the mutants PSII properties. A tobacco mutant, S6, obtained by Maliga and coworkers harboring the F26S mutation in the b subunit was made available to us and was characterized. Measurements of PSII charge separation and recombination, polypeptide content and electron flow indicates that this mutation indeed results in light sensitivity. Presently further work is in progress in the detailed characterization of the properties of all the above mutants. Information was obtained demonstrating that photoinactivation of PSII in vivo initiates a series of progressive changes in the properties of RCII which result in an irreversible modification of the RCII-D1 protein leading to its degradation and replacement. The cleavage process of the modified RCII-D1 protein is regulated by the occupancy of the QB site of RCII by plastoquinone. Newly synthesized D1 protein is not accumulated in a stable form unless integrated in reassembled RCII. Thus the degradation of the irreversibly modified RCII-D1 protein is essential for the recovery process. The light induced degradation of the RCII-D1 protein is rapid in mutants lacking the pD1 processing protease such as in the LF-1 mutant of the unicellular alga Scenedesmus obliquus. In this case the Mn binding site of PSII is abolished, the water oxidation process is inhibited and harmful cation radicals are formed following light induced electron flow in PSII. In such mutants photo-inactivation of PSII is rapid, it is not protected by ligands binding at the QB site and the degradation of the inactivated RCII-D1 occurs rapidly also in the dark. Furthermore the degraded D1 protein can be replaced in the dark in absence of light driven redox controlled reactions. The replacement of the RCII-D1 protein involves the de novo synthesis of the precursor protein, pD1, and its processing at the C-terminus end by an unknown processing protease. In the frame of this work, a gene previously isolated and sequenced by Dr. Pakrasi's group has been identified as encoding the RCII-pD1 C-terminus processing protease in the cyanobacterium Synechocystis sp. PCC 6803. The deduced sequence of the ctpA protein shows significant similarity to the bovine, human and insect interphotoreceptor retinoid-binding proteins. Results obtained using C. reinhardtii cells exposes to low light or series of single turnover light flashes have been also obtained indicating that the process of RCII-D1 protein turnover under non-photoinactivating conditions (low light) may be related to charge recombination in RCII due to back electron flow from the semiquinone QB- to the oxidised S2,3 states of the Mn cluster involved in the water oxidation process.

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