ferricytochrome c oxidoreductase . Other names in common use include coenzymeQcytochromecreductase, dihydrocoenzyme Qcytochromecreductase, reduced ubiquinone cytochromecreductase, complex III, mitochondrial electron transport , ubiquinone cytochromecreductase, ubiquinol cytochromec oxidoreductase, reduced coenzymeQcytochromecreductase, ubiquinone cytochromec oxidoreductase, reduced ubiquinone cytochromec oxidoreductase, mitochondrial electron transport complex III, ubiquinol cytochromec 2 oxidoreductase, ubiquinone cytochrome b c1 oxidoreductase, ubiquinol cytochrome c2 reductase, ubiquinol cytochrome c1 oxidoreductase, CoQH2 cytochromec oxidoreductase, ubihydroquinol cytochromec oxidoreductase, coenzyme QH2 cytochromecreductase, and QH2 cytochromec oxidoreductase ... complexes in membranes MeshName CoenzymeQCytochromecReductase Diphenol family oxidoreductases ... illustration of complex III reactions The coenzymeQcytochromec oxidoreductase , sometimes called ... Coenzima Q citocromo c reductasa fr CoenzymeQcytochromec r ductase id Koenzim Q sitokrom c reduktase ... CAZy CDD enzyme Name ubiquinol cytochromecreductase EC number 1.10.2.2 CAS number 9027 03 6 IUBMB ... cytochromecreductase catalyzes the chemical reaction QH sub 2 sub 2 ferricytochrome c math rightleftharpoons math Q 2 ferrocytochrome c 2 H sup sup Thus, the two substrate biochemistry substrates of this enzyme are dihydroquinone QH2 and ferri Fe sup 3 sup cytochromec , whereas its 3 product chemistry products are quinone Q , ferro Fe sup 2 sup cytochromec, and hydrogen ion H sup sup ... c by oxidation of coenzymeQ CoQ and the concomitant pumping of 4 protons from the mitochondrial ... in sub Q 2 cytochromec Fe sup II sup 4 H sup sup sub out sub In the process called Q cycle , ref name ... thumb 400px The Q cycle The reaction mechanism for complex III Cytochrome bc1, CoenzymeQCytochrome ... L sub and b sub H sub , the cytochromec subunit has one c type heme Cytochrome C1 c sub 1 sub , and the Rieske ... more details
enzyme Name iron cytochromecreductase EC number 1.9.99.1 CAS number 37256 52 3 IUBMB EC number 1 9 99 1 GO code 0047726 image width caption In enzymology , an iron cytochromecreductase EC number 1.9.99.1 is an enzyme that catalysis catalyzes the chemical reaction ferrocytochrome c Fe sub 3 sub math rightleftharpoons math ferricytochrome c Fe sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are ferrocytochrome c and Fe3 , whereas its two product chemistry products are ferricytochrome c and Fe2 . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a heme group of donors with other acceptors. The systematic name of this enzyme class is ferrocytochrome c Fe3 oxidoreductase . This enzyme is also called iron cytochromecreductase . It employs one cofactor biochemistry cofactor , iron . References reflist 1 cite journal author Yates MG, Nason A date 1966 title Electron transport systems of the chemoautotroph Ferrobacillus ferrooxidans. II. Purification and properties of a heat labile iron cytochromecreductase journal J. Biol. Chem. volume 241 pages 4872&ndash 80 pmid 4288725 issue 21 1.9 enzyme stub Category EC 1.9.99 Category Iron enzymes Category Enzymes of unknown structure it Ferro citocromo c reduttasi ja c ... more details
enzyme Name Cytochromec nitrite reductase EC number 1.7.2.2 CAS number IUBMB EC number 1 7 2 2 GO code 0042279 image 1GU6.png PDB 1GU6 width caption X ray crystallography Biological macromolecular crystallography Crystallographic structure of a protein dimer homodimer of the cytochromec nitrite reductase from Escherichia coli rainbow colored cartoon, blue N terminus , red C terminus complexed with heme C sticks . ref name pmid11863430 PDB 1GU6 cite journal author Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ title Structure and spectroscopy of the periplasmic cytochromec nitrite reductase from Escherichia coli journal Biochemistry volume 41 issue 9 pages 2921 31 year 2002 month March pmid 11863430 doi 10.1021 bi015765d ref Cytochromec nitrite reductase ccNiR EC number 1.7.2.2 is a bacterial enzyme that catalysis catalyzes the six electron Organic redox reaction reduction of nitrite to ammonia an important step in the biological nitrogen cycle . ref name pmid18433623 cite journal author Clarke TA, Mills PC, Poock SR, Butt JN, Cheesman MR, Cole JA, Hinton JC, Hemmings AM, Kemp G, S derberg CA, Spiro S, Van Wonderen J, Richardson DJ title Escherichia coli cytochromec nitrite reductase NrfA journal Meth. Enzymol. volume 437 issue pages ... 10.1111 j.1574 6976.2002.tb00616.x ref Cytochromec Nitrite Reductase is a homodimer which contains five heme cc type heme cofactors per monomer. ref name pmid10440380 cite journal author Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM title Structure of cytochromec nitrite reductase journal Nature volume 400 issue 6743 pages 476 80 year 1999 month July pmid ... GP, Bartunik HD, Huber R, Kroneck PM title Structure of cytochromec nitrite reductase journal ... on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is ammonia ferricytochrome c oxidoreductase . Structural studies The crystal structure ... more details
enzyme Name trimethylamine N oxide reductasecytochromec EC number 1.7.2.3 CAS number 37256 34 1 IUBMB EC number 1 7 2 3 GO code 0050626 image width caption In enzymology , a trimethylamine N oxide reductasecytochromec EC number 1.7.2.3 is an enzyme that catalysis catalyzes the chemical reaction trimethylamine 2 ferricytochrome c subunit H sub 2 sub O math rightleftharpoons math trimethylamine N oxide 2 ferrocytochrome c subunit 2 H sup sup The 3 substrate biochemistry substrates of this enzyme are trimethylamine , ferricytochrome c subunit , and water H sub 2 sub O , whereas its 3 product chemistry products are trimethylamine N oxide , ferrocytochrome c subunit , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is trimethylamine cytochromec oxidoreductase . Other names in common use include TMAO reductase , and TOR . This enzyme participates in two component system general . References reflist 1 cite journal author Arata H, Shimizu M, Takamiya K date Tokyo title Purification and properties of trimethylamine N oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans journal J. volume Biochem. pages 470&ndash 5 pmid 1337081 issue 4 cite journal doi 10.1515 bchm.1997.378.3 4.293 author Knablein J, Dobbek H, Ehlert S, Schneider F date 1997 title Isolation, cloning, sequence analysis and X ray structure of dimethyl sulfoxide trimethylamine N oxide reductase from Rhodobacter capsulatus ... author Gon S, Giudici Orticoni MT, Mejean V, Iobbi Nivol C date 2001 title Electron transfer and binding of the c type cytochrome TorC to the trimethylamine N oxide reductase in Escherichia coli journal ... trimethylamine N oxide reductase from Shewanella massilia at 2.5 A resolution journal J. Mol ... reduttasi citocromo c ja N c ... more details
between CoenzymeQcytochromecreductase Complexes III CoenzymeQ Cyt Creductase and cytochromec oxidase IV Cyt C oxidase . In humans, cytochromec is encoded by the CYCS gene . ref name entrez cite web title Entrez Gene cytochromec url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ...PBB geneid 54205 The Cytochrome complex , or cyt c is a small heme protein found loosely associated with the inner membrane of the mitochondrion . It belongs to the cytochromec family of proteins. Cytochromec is a highly soluble protein, unlike other cytochrome s, with a solubility of about 100 g L ... NO, Hurster KA, Pastorino JG, Schneider T, Russo MA, Farber JL title Cytochromec release upon ... month March pmid 11790791 doi 10.1074 jbc.M111350200 url ref Function Cytochromec is a component of the electron transport chain in mitochondria. The heme group of cytochromec accepts electrons from the b c1 complex and transfers electrons to the cytochrome oxidase complex. Cytochromec is also involved in initiation of apoptosis . Upon release of cytochromec to the cytoplasm, the protein binds apoptotic protease activating factor 1 Apaf 1 . ref name entrez Cytochromec can catalyze several ... 4 thiomethyl butyric acid and 4 aminoantipyrine. Species distribution Cytochromec is a highly conserved ... ensiweb lessons molb.ws.pdf Amino acid sequences in cytochromec proteins from different species , adapted from Strahler, Arthur Science and Earth History, 1997. page 348. ref The cytochromec molecule .... ref name indiana Pig s, cow s and sheep also share identical cytochromec molecules. ref name indiana Classes In 1991 R. P. Ambler recognized four classes of cytochromec ref name pmid1646017 ... 05 80266 X url ref Class I includes the lowspin soluble cytochromec of mitochondria and bacteria ... by a methionine residue towards the C terminus. Class II includes the highspin cytochromec . It has ... to hold the complex proteins that have other prosthetic groups as well as heme c. Applications Cytochrome ... more details
PBB geneid 5447 Cytochrome P450 reductase EC number 1.6.2.4 also known as NADPH ferrihemoprotein oxidoreductase, NADPH hemoprotein oxidoreductase, NADPH P450 oxidoreductase, P450 reductase, POR , CPR, CYPOR is a membrane bound enzyme required for electron transfer to cytochrome P450 in the microsome ... NADPH cytochrome P450 reductase POR EC number 1.6.2.4 . Introduction In Bacillus megaterium and Bacillus subtilis , POR is a C terminal domain of CYP102, a single polypeptide self sufficient soluble ... 97 00418 7 author Lesuisse, E., Casteras Simon, M. and Labbe, P. title Cytochrome P 450 reductase is responsible ... and functional analysis of NADPH cytochrome P 450 reductase from human liver complete sequence ... Restoration of mutant cytochrome P450 reductase activity by external flavin journal Mol. Cell. Endocrinol ... L, Ding X title Transgenic mice with a hypomorphic NADPH cytochrome P450 reductase gene effects ... systems References Reflist 2 External links MeshName Cytochrome P450 Reductase http www.ncbi.nlm.nih.gov ... no DEFAULTSORT Cytochrome P450 Reductase Category Cytochrome P450 ... in cytochrome P450 mediated reactions came from the work of Lu, Junk and Coon, ref cite journal author Lu, A.Y.H., Junk, K.W. and Coon, M.J. title Resolution of the cytochrome P 450 containing &omega ... system into three constituent components POR, cytochrome P450, and lipids. Since all microsomal ... with loss of microsomal NADPH cytochrome P450 oxidoreductase journal J. Biol. Chem. volume 277 issue ... of hepatic drug metabolism. ref cite journal author Gu, J., Weng, Y., Zhang, Q. Y., Cui, H., Behr, M., Wu, L., Yang, W., Zhang, L. and Ding, X. title Liver specific deletion of the NADPH cytochrome P450 reductase gene. Impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase journal J. Biol. Chem. volume 278 issue 28 pages 25895 25901 year 2003 pmid 12697746 doi 10.1074 jbc.M303125200 ref The reduction of cytochrome P450 is not the only ... more details
enzyme Name cytochrome b5 reductase EC number 1.6.2.2 CAS number 9032 25 1 IUBMB EC number 1 6 2 2 GO code 0004128 image NADH cytochrome B5 reductase 1UMK.png width caption Ribbon diagram of red blood cell erythrocytic methemoglobin reductase with FAD bound. From PDB 1UMK . Cytochrome b sub 5 sub reductase also known as methemoglobin reductase is a NADH dependent enzyme that converts methemoglobin to hemoglobin . It contains FAD and catalyzes the reaction center NADH H sup sup 2 ferricytochrome b sub 5 sub NAD sup sup 2 ferrocytochrome b sub 5 sub center The following four human genes encode cytochrome b sub 5 sub reductases CYB5R1 CYB5R2 CYB5R3 CYB5R4 See also Cytochrome b5 Methemoglobinemia Reductase External links MeshName Cytochrome B 5 Reductase PDB 1IB0 crystal structure of rat CBR complexed with NAD PDB 1NDH crystal structure of pig liver CBR PDB 1UMK crystal structure of human erythrocyte CBR InterPro IPR001834 InterPro entry for CBR NADH or NADPH oxidoreductases Flavoproteins Category EC 1.6.2 de Cytochrom b5 Reduktasen it Citocromo b5 reduttasi ja b5 zh b5 ... more details
enzyme Name cytochromec methionine S methyltransferase EC number 2.1.1.123 CAS number 93585 98 9 IUBMB EC number 2 1 1 123 GO code 0030783 image width caption In enzymology , a cytochromec methionine S methyltransferase EC number 2.1.1.123 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine cytochromec methionine math rightleftharpoons math S adenosyl L homocysteine cytochromec S methyl methionine Thus, the two substrate biochemistry substrates of this enzyme are S Adenosyl methionine S adenosyl methionine and cytochromec methionine , whereas its two product chemistry products are S adenosylhomocysteine and cytochromec S methyl methionine . This enzyme belongs to the family of transferase s, specifically those transferring one carbon group methyltransferases. The systematic name of this enzyme class is S adenosyl L methionine cytochromec methionine S methyltransferase . References reflist 1 cite journal author Farooqui JZ, Tuck M, Paik WK year 1985 title Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochromec journal J. Biol. Chem. volume 260 pages 537&ndash 45 pmid 2981218 issue 1 DEFAULTSORT CytochromeC Methionine S Methyltransferase Category EC 2.1.1 Category Enzymes of unknown structure transferase stub it citocromo c metionina S metiltransferasi ... more details
enzyme Name Cytochromec oxidase EC number 1.9.3.1 CAS number 9001 16 5 IUBMB EC number 1 9 3 1 GO code 0009485 image CytochromeC Oxidase 1OCC in Membrane 2.png width 296px caption The crystal structure of bovine cytochromec oxidase in a phospholipid bilayer. The intermembrane space lies to top of the image ... transport chain. Complex IV is at the right. The enzyme cytochromec oxidase or Complex IV PDB ... bovine heart cytochromec oxidase at 2.8 A journal Science volume 269 issue 5227 pages 1069 ... 3 sub and Cu sub B sub form a binuclear center that is the site of oxygen reduction. Cytochromec reduced ... c containing Fe sup 3 sup . The reduced Cu sub A sub binuclear center now passes an electron on to cytochrome ... ion in the fully oxidized state. X ray crystallography Crystallographic studies of cytochromec oxidase ... Biogenesis of cytochromec oxidase journal Mitochondrion volume 5 issue 6 pages 363 88 year 2005 month ... Fontanesi F, Soto IC, Horn D, Barrientos A title Assembly of mitochondrial cytochromec oxidase ... Biochemistry Summary reaction 4 Fe sup 2 sup cytochromec 8 H sup sup sub in sub O sub 2 sub 4 Fe sup 3 sup cytochromec 2 H sub 2 sub O 4 H sup sup sub out sub Two electrons are passed from two cytochromec s, through the Cu sub A sub and cytochrome a sites to the cytochrome a sub 3 sub Cu sub B sub ... up two electrons and a proton. A third electron arising from another cytochromec is passed through ... sub B sub sup 2 sup to a water molecule. The fourth electron from another cytochromec flows through ... cytochromec oxidase of human mitochondrial respiratory chain journal Pharmacol. Toxicol. volume ... ref all bind to cytochromec oxidase, thus competitive inhibition competitively inhibiting the protein ... defects and disorders Defects involving genetic mutations altering cytochromec oxidase COX functionality ... H, Hans kov H, Zeman J, Houstek J title Genetic defects of cytochromec oxidase assembly journal ... See also Cytochromec oxidase subunit I Cytochromec oxidase subunit II Cytochromec oxidase subunit ... more details
enzyme Name cytochromec peroxidase EC number 1.11.1.5 IUBMB EC number 1 11 1 5 CAS number 9029 53 2 GO code 0004130 image width caption Cytochromec peroxidase , or CCP is a water soluble heme containing enzyme of the peroxidase family that takes reducing equivalents from cytochromeccytochromec and reduces hydrogen peroxide to water CCP H sub 2 sub O sub 2 sub 2 ferrocytochrome c 2H sup sup CCP 2H sub 2 sub O 2 ferricytochrome cCytochromec peroxidase can react with hydroperoxides other than hydrogen peroxide, but the reaction rate is much slower than with hydrogen peroxide. It was first isolated from baker s yeast by R. A. Altschul, Abrams, and Hogness in 1940, ref Altchul, A. M., Abrams, R., and Hogness, T. R. 1940 Cytochromec peroxidase. J. Biol. Chem., 136, 777. ref though not to purity. The first purified preparation of yeast CCP dates to Takashi Yonetani and his preparation by ion exchange chromatography in the early 1960s. The X ray crystallography X ray structure was the work of Thomas Poulos and coworkers in the late 1970s. ref Poulos, T. L., Freer, S. T., Alden, R. A., Edwards, S. L., Skogland, U., Takio, K., Eriksson, B., Xuong, N., Yonetani, T., and Kraut, J. 1980 http www.jbc.org content 255 2 575.full.pdf The crystal structure of cytochromec peroxidase. J. Biol. Chem. 255, 575 580. ref The yeast enzyme is a monomer of molecular weight 34,000, containing 293 amino acids, and contains as well a single noncovalently bound heme b . Unusual for proteins, this enzyme crystallizes when dialysis biochemistry dialysed against distilled water. More so, the enzyme ... step. Much like catalase , the reaction of cytochromec peroxidase proceeds through a three ... faculty.ucsd.edu kraut projects.html Cytochromec peroxidase , maintained by the http chem faculty.ucsd.edu ... entry for yeast cytochromec peroxidase. Peroxidases DEFAULTSORT CytochromeC Peroxidase Category EC 1.11.1 Category Hemoproteins it Citocromo c perossidasi ja c ... more details
Pfam box Symbol Cytochrom C Name Cytochromec image PDB 1cry EBI.jpg width caption Structure of cytochrome ... family Symbol Cytochrom C 2 Name CytochromeC image PDB 1bbh EBI.jpg width caption atomic structure of a cytochromec with an unusual ligand controlled dimer dissociation at 1.8 angstroms resolution ... OPM protein CAZy CDD Infobox protein family Symbol Cytochrom CIII Name Class III cytochromeC family ... of the 16 heme cytochromec hmca at 2.5 a resolution and a view of its role in transmembrane ... issue pages year 1987 ref . The founding member of this family is cytochromec mitochondrial cytochromec . Ambler ref name PUB00000610 cite journal author Ambler RP title Sequence variability in bacterial cytochromes c journal Biochim. Biophys. Acta volume 1058 issue 1 pages 42 47 year 1991 pmid ... of a cytochromec with an unusual ligand controlled dimer dissociation at 1.8 A resolution journal ... c and cytochromes cd. ref name PUB00000610 Subfamilies Bacterial cytochromec, class IC InterPro IPR008169 Human proteins containing this domain Cytochromec CYCS References reflist InterPro ... analysis of cytochrome c2 from Rhodopseudomonas viridis journal Acta Crystallogr. D Biol. Crystallogr ... 119 PDB3 1i8o A 28 139 PDB3 1i8p A 28 139 PDB3 1fj0 C 28 139 PDB3 1hh7 A 28 139 PDB3 1qn2 B 4 100 ... X 25 139 PDB3 1cot 25 139 PDB3 155c 25 137 PDB3 1w2l A 223 316 PDB3 2c8s A 79 157 PDB3 2mta C 68 ... PDB3 1hzu A 61 138 PDB3 1dt1 A 20 108 PDB3 1foc A 1 91 PDB3 1qyz A 1 91 PDB3 1c52 C 1 91 PDB3 1r0q ... OPM family OPM protein CAZy CDD Cytochromes c cytC are electron transfer proteins having one or several heme c groups, bound to the protein by one or, more generally, two thioether bonds involving ... residue. Cytochromes c possess a wide range of properties and function in a large number of different ... the C terminus. On the basis of sequence similarity, class I cytC were further subdivided into five ... IB cytC. Class II includes the high spin cytC and a number of low spin cytochromes, e.g. cyt c ... more details
Image Cytochrome c.png thumb 250px Cytochromec with heme c . Cytochromes are, in general, membrane bound ... as Protein subunit monomeric protein s e.g., cytochromec or as Protein subunit subunits of bigger ..., the pyridine hemochrome method. Within each class, cytochrome a , b , or c , early cytochromes are numbered consecutively, e.g. cyt c , cyt c sub 1 sub , and cyt c sub 2 sub , with more recent examples designated by their reduced state R band maximum, e.g. cyt c sub 559 sub . ref name pmid14871137 cite journal author Reedy, C. J. & Gibney, B. R. title Heme protein assemblies journal Chem Rev volume ... types of cytochrome are distinguished by their prosthetic groups class wikitable Type prosthetic group Cytochrome a heme a Cytochrome b heme b Cytochrome d tetrapyrrolic chelate of iron ref MeshName Cytochrome d ref The definition of cytochromec is not defined in terms of the heme group. ref MeshName Cytochromec Group . ref There is no cytochrome e, but there is a cytochrome f , which is often considered a type of cytochromec. ref eMedicineDictionary Cytochrome ref In mitochondrion mitochondria ... 10.1098 rstl.1886.0007 jstor 109482 pages 267 298 author1 Mac Munn, C. A issue 0 title Researches ... a 605 nm , b 565 nm , and c 550 nm . The UV visible spectroscopic signatures ... of flagellum flagella . Types Several kinds of cytochrome exist and can be distinguished by spectroscopy ... and related metabolic pathways class wikitable Cytochromes Combination a and a sub 3 sub Cytochromec oxidase Complex IV with electrons delivered to complex by soluble cytochromec hence the name b and Cytochrome C1 c sub 1 sub CoenzymeQcytochromecreductase Complex III b sub 6 sub and Cytochrome f f Plastoquinol plastocyanin reductase A completely distinct family of cytochromes is known as the cytochrome P450 oxidase s, so named for the characteristic Soret peak formed by absorbance ... de Cytochrome es Citocromo eo Citokromo eu Zitokromo fa fr Cytochrome id Sitokrom it Citocromi ... more details
Pfam box Symbol COX1 Name CytochromeC and Quinol oxidase polypeptide I image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromec oxidase. ref name pmid8638158 cite journal author Tsukihara T, Aoyama H, Yamashita E, et al. title The whole structure of the 13 subunit oxidized cytochromec oxidase at 2.8 A journal Science volume 272 issue 5265 pages 1136 44 year 1996 month May pmid 8638158 doi 10.1126 science.272.5265.1136 url bibcode 1996Sci...272.1136T ref Pfam PF00115 InterPro IPR000883 SMART PROSITE PDOC00074 SCOP 1occ TCDB 3.D.4 OPM family 4 OPM protein 1v55 CDD cd01663 PDB PDB3 2occ N 5 461 PDB3 1ocr N 5 461 PDB3 1v54 A 5 461 PDB3 1occ A 5 461 PDB3 1v55 A 5 461 ... 1ehk A 218 309 PDB3 1fft A 47 505 PDB3 1xme A 18 108 CytochromeC and Quinol oxidase polypeptide I is main subunit of cytochromec oxidase complex. Cytochromec oxidase EC number 1.9.3.1 is a key enzyme ..., associated with the largest subunit I of cytochromec and ubiquinol oxidases EC number 1.10.3 ... author Capaldi RA, Malatesta F, Darley Usmar VM title Structure of cytochromec oxidase journal Biochim ... quinol oxidase was derived from cytochromec oxidase in Gram positive bacteria and that archaebacterial ... Gram positive bacteria. ref name PUB00002253 A related nitric oxide reductase EC number 1.7.99.7 exists in denitrifying species of archae and eubacteria and is a heterodimer of cytochromes b and c. Phenazine methosulphate can act as acceptor. Subfamilies Cytochromec oxidase cbb3 type, subunit I InterPro IPR004677 Cytochrome o ubiquinol oxidase, subunit I InterPro IPR014207 Cytochrome aa3 quinol oxidase, subunit I InterPro IPR014233 Cytochromec oxidase, subunit I bacterial type InterPro IPR014241 Examples In humans, the main subunit of cytochromec oxidase is encoded by the MT CO1 gene. References ... cite journal author Saraste M, Castresana J, Higgins DG, Lubben M title Evolution of cytochrome ... cite journal author Saraste M, Holm L, Wikstrom M title Structural models of the redox centres in cytochrome ... more details
enzyme Name cytochromec arginine N methyltransferase EC number 2.1.1.124 CAS number 9055 07 6 IUBMB EC number 2 1 1 124 GO code 0016275 image width caption In enzymology , a cytochromec arginine N methyltransferase EC number 2.1.1.124 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine cytochromec arginine math rightleftharpoons math S adenosyl L homocysteine cytochromec Nomega methyl arginine Thus, the two substrate biochemistry substrates of this enzyme are S Adenosyl methionine S adenosyl methionine and cytochromec arginine , whereas its two product chemistry products are S adenosylhomocysteine and cytochromec Nomega methyl arginine . This enzyme belongs to the family of transferase s, specifically those transferring one carbon group methyltransferases. The systematic name of this enzyme class is S adenosyl L methionine cytochromec arginine Nomega methyltransferase . Other names in common use include S adenosyl L methionine cytochromec arginine , and omega N methyltransferase . References reflist 1 cite journal author Farooqui JZ, Tuck M, Paik WK year 1985 title Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochromec journal J. Biol. Chem. volume 260 pages 537&ndash 45 pmid 2981218 issue 1 DEFAULTSORT CytochromeC Arginine N Methyltransferase Category EC 2.1.1 Category Enzymes of unknown structure transferase stub it citocromo c arginina N metiltransferasi ... more details
enzyme Name cytochromec lysine N methyltransferase EC number 2.1.1.59 CAS number 82047 78 7 IUBMB EC number 2 1 1 59 GO code 0000277 image width caption In enzymology , a cytochromec lysine N methyltransferase EC number 2.1.1.59 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine cytochromec L lysine math rightleftharpoons math S adenosyl L homocysteine cytochromec N sub 6 sub methyl L lysine Thus, the two substrate biochemistry substrates of this enzyme are S Adenosyl methionine S adenosyl methionine and cytochromec L lysine , whereas its two product chemistry products are S adenosylhomocysteine and cytochromec N6 methyl L lysine . This enzyme belongs to the family of transferase s, specifically those transferring one carbon group methyltransferases. The systematic name of this enzyme class is S adenosyl L methionine cytochromec L lysine N6 methyltransferase . Other names in common use include cytochromec lysine methyltransferase , cytochromec methyltransferase , cytochromec specific protein methylase III , cytochromec specific protein lysine methyltransferase , S adenosyl L methionine cytochromec L lysine , and 6 N methyltransferase . This enzyme participates in lysine degradation . References reflist 1 cite journal author Durban E, Nochumson S, Kim S, Paik WK, Chan SK year 1978 title Cytochromec specific protein lysine methyltransferase from Neurospora crassa. Purification, characterization, and substrate requirements journal J. Biol ... E, Kim S, Paik WK year 1977 title Cytochromec specific protein methylase III from Neurospora crassa ... Valentine J, Pettigrew GW year 1982 title A cytochromec methyltransferase from Crithidia oncopelti journal Biochem. J. volume 201 pages 329&ndash 38 pmid 6282265 issue 2 pmc 1163647 DEFAULTSORT CytochromeC Lysine N Methyltransferase Category EC 2.1.1 Category Enzymes of unknown structure transferase stub it citocromo c lisina N metiltransferasi ... more details
Pfam box Symbol COX3 Name Cytochromec oxidase subunit III image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromec oxidase. ref name pmid15299438 cite journal author Miki K title Application of an automatic molecular replacement procedure to crystal structure analysis of cytochrome ... 12 17 PDB3 1v55 C 6 261 PDB3 1occ P 6 261 PDB3 1oco C 6 261 PDB3 1ocz C 6 261 PDB3 1ocr P 6 261 PDB3 2occ C 6 261 PDB3 1v54 C 6 261 PDB3 1llk A 6 261 PDB3 1m56 I 7 266 PDB3 1m57 I 7 266 PDB3 1qle C 7 273 PDB3 1fft H 1 203 Cytochromec oxidase subunit III is one of main transmembrane subunits of cytochromec oxidase Cytochromec oxidase EC number 1.9.3.1 is the terminal enzyme of the respiratory chain ... c to molecular oxygen 4 cytochromec sup 2 sup 4 H sup sup O sub 2 sub math rightleftharpoons math 4 cytochromec sup 3 sup 2 H sub 2 sub O This reaction is coupled to the pumping of four additional ... Michel H title Cytochromec oxidase catalytic cycle and mechanisms of proton pumping a discussion ... coupled electron transfer drives the proton pump of cytochromec oxidase journal Nature volume 440 issue 7085 pages 829 32 year 2006 pmid 16598262 doi 10.1038 nature04619 ref . Cytochromec oxidase ... cytochromec oxidase contains three common subunits, Cytochromec oxidase subunit I I , Cytochrome ... are branched, they have a number of distinct terminal oxidases, rather than the single cytochromec ... the cytochromec but the quinol ubiquinol oxidation they belong to the same haem copper oxidase superfamily as cytochromec oxidases. Members of this family share sequence similarities in all three core subunits Cytochromec oxidase subunit I subunit I is the most conserved subunit, whereas Cytochromec oxidase subunit II subunit II is the least conserved ref name PUB00006601 cite journal ... oxidase of Escherichia coli and the aa3 type family of cytochromec oxidases journal J. Biol. Chem ... subunit oxidized cytochromec oxidase at 2.8 A. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi ... more details
drive Adenosine triphosphate ATP synthesis. In its structure and functions, the cytochrome bc1 complex cytochrome bc1 complex bears extensive analogy to the cytochromeCytochrome b6f complex b6f complex of chloroplast s and cyanobacteria cyt c1 plays an analogous role to cytochrome f, in spite of their different structures. ref name pmid7631417 cite journal author Prince RC, George GN title Cytochrome ... 7631417 doi url ref External links MeshName Cytochrome c1 References reflist InterPro content IPR002326 ... more details
Orphan date February 2009 Pfam box Symbol COX5B Name Cytochromec oxidase subunit Vb image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromec oxidase. ref name pmid15299438 cite journal author Miki K, Sogabe S, Uno A, et al. title Application of an automatic molecular replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis journal Acta Crystallogr. D Biol. Crystallogr. volume 50 issue Pt 3 pages 271 5 year 1994 month May pmid 15299438 doi 10.1107 S0907444993013952 url ref Pfam PF01215 InterPro IPR002124 SMART PROSITE PDOC00663 SCOP 1occ TCDB OPM family 4 OPM protein 1v55 PDB PDB3 1v55 S 30 98 PDB3 1occ S 30 98 PDB3 1v54 F 30 98 PDB3 1oco F 30 98 PDB3 1ocz S 30 98 PDB3 1ocr F 30 98 PDB3 2occ S 30 98 Cytochromec oxidase, subunit Vb is a subunit of mitochondrial cytochromec oxidase complex. Cytochromec oxidase EC number 1.9.3.1 is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochromec to oxygen. ref name PUB00000581 cite journal author Capaldi RA, Malatesta F, Darley Usmar VM title Structure of cytochromec oxidase journal Biochim. Biophys. Acta volume 726 issue 2 pages 135 148 year 1983 pmid 6307356 ref In eukaryotes this enzyme complex is located in the mitochondrial inner membrane in aerobic prokaryotes it is found in the plasma membrane. In eukaryotes, in addition to the three large subunits, I, II and III, that form ... of the 13 subunit oxidized cytochromec oxidase at 2.8 A journal Science volume 272 issue 5265 ...?PDOC00663 Cytochromec oxidase subunit Vb in PROSITE InterPro content IPR002124 Category Protein ... R, Sandona D, Brini M, Capaldi RA, Bisson R title The most conserved nuclear encoded polypeptide of cytochromec oxidase is the putative zinc binding subunit primary structure of subunit V from the slime ... ref Two of these cysteines are clustered in the C terminal section of the subunit. Human proteins ... more details
Pfam box Symbol COX2 TM Name Cytochromec oxidase subunit II, transmembrane domain image 1qle opm.gif width 250 caption Bacterial cytochromec oxidase complex. Subunit II indicated by blue. Pfam PF02790 InterPro IPR011759 SMART PROSITE PDOC00075 SCOP 1occ TCDB 3.D.4 OPM family 4 OPM protein 1v55 PDB PDB3 1v54 B 2 83 PDB3 1ocz B 1 83 PDB3 2occ B 1 83 PDB3 1ocr B 1 83 PDB3 1oco B 1 83 PDB3 1v55 B 2 83 PDB3 1occ O 1 83 PDB3 1m57 B 35 122 PDB3 1m56 H 35 122 PDB3 1qle B 41 128 Pfam box Symbol COX2 Name CytochromeC oxidase subunit II, periplasmic domain image width caption Pfam PF00116 InterPro IPR002429 SMART PROSITE PDOC00075 SCOP 1occ TCDB 3.D.4 OPM family 4 OPM protein 1v55 PDB PDB3 1v54 B 95 214 PDB3 1ocz B 95 214 PDB3 2occ B 95 214 PDB3 1ocr B 95 214 PDB3 1oco B 95 214 PDB3 1v55 B 95 214 PDB3 ... 1cyw 129 225 PDB3 1cyx 129 225 PDB3 1fwx C 572 648 PDB3 1qni B 489 579 PDB3 1ehk B 92 167 PDB3 2cua A 59 134 PDB3 1xme B 59 134 Cytochromec oxidase subunit II , abbreviated CoxII , is the second subunit of cytochromec oxidase . Cytochromec oxidase EC number 1.9.3.1 ref name PUB00000581 cite journal author Capaldi RA, Malatesta F, Darley Usmar VM title Structure of cytochromec oxidase journal ... chain and is involved in the transfer of electrons from cytochromec to oxygen. In eukaryotes ... Cu A see InterPro IPR001505 , probably the primary acceptor in cytochromec oxidase. An exception is the corresponding ... CO II have a C terminal extension that contains a covalently bound haem c. The N terminal domain of cytochromeC oxidase contains two transmembrane alpha helices. Human proteins containing this domain ... oxidized cytochromec oxidase at 2.8 A. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H ... polypeptides mammals . In Leigh s disease , there may be an abnormality or deficiency of cytochrome oxidase. Subunit 2 CO II transfers the electrons from cytochromec to the Main subunit of cytochromec oxidase catalytic subunit 1 . It contains two adjacent transmembrane regions in its N terminus and the major ... more details
Infobox protein family Symbol Cytochrom C asm Name CytochromeC assembly protein image width caption Pfam PF01578 Pfam clan CL0328 InterPro IPR002541 SMART PROSITE MEROPS SCOP TCDB 9.B.14 OPM family OPM protein CAZy CDD In molecular biology, the cytochromec assembly protein family includes various protein s involved in cytochromec assembly from mitochondria and bacteria. Members of this family include CycK from Rhizobium leguminosarum , ref name pmid7665469 cite journal author Delgado MJ, Yeoman KH, Wu G, Vargas C, Davies AE, Poole RK, Johnston AW, Downie JA title Characterization of the cycHJKL genes involved in cytochromec biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum journal J. Bacteriol. volume 177 issue 17 pages 4927 34 year 1995 month September pmid 7665469 pmc 177267 doi url ref CcmC from Escherichia coli and Paracoccus denitrificans , ref name pmid7635817 cite journal author Thony Meyer L, Fischer F, K nzler P, Ritz D, Hennecke H title Escherichia coli genes required for cytochromec maturation journal J. Bacteriol. volume 177 issue 15 pages 4321 6 ... Page MD, Pearce DA, Norris HA, Ferguson SJ title The Paracoccus denitrificans ccmA, B and C genes cloning and sequencing, and analysis of the potential of their products to form a haem or apo c type cytochrome .... This transporter may be necessary for transport of some component needed for cytochromec assembly ... name pmid7665469 cite journal author Delgado MJ, Yeoman KH, Wu G, Vargas C, Davies AE, Poole RK, Johnston AW, Downie JA title Characterization of the cycHJKL genes involved in cytochromec biogenesis ... DA, Norris HA, Ferguson SJ title The Paracoccus denitrificans ccmA, B and C genes cloning and sequencing, and analysis of the potential of their products to form a haem or apo c type cytochrome transporter ... a putative haem binding motif and is a proposed ABC transporter with c type haem as its proposed ... it seems unlikely that all members of this family transport haem or c type apocytochromes because ... more details
Infobox protein family Symbol CCP MauG Name Di haem cytochromec peroxidase image PDB 1eb7 EBI.jpg width caption crystal structure of the di haem cytochromec peroxidase from pseudomonas aeruginosa Pfam PF03150 Pfam clan CL0318 InterPro IPR004852 SMART PROSITE MEROPS SCOP 1eb7 TCDB OPM family OPM protein CAZy CDD In molecular biology, the di haem cytochromec peroxidase family is a group of distinct cytochromec peroxidase cytochromec peroxidases CCPs that contain two haem groups. Similar to other cytochromec peroxidases, they reduce hydrogen peroxide to water using c type haem as an oxidizable Enzyme substrate substrate . However, since they possess two, instead of one, haem prosthetic groups , this family of bacteria bacterial CCPs reduce hydrogen peroxide without the need to generate semi stable free radical s. The two haem groups have significantly different redox potentials. The high potential 320 mV haem feeds electron s from electron shuttle protein s to the low potential 330 mV haem, where peroxide is Redox reduced indeed, the low potential site is known as the peroxidatic site . ref name pmid8591033 cite journal author Fulop V, Ridout CJ, Greenwood C, Hajdu J title Crystal structure of the di haem cytochromec peroxidase from Pseudomonas aeruginosa journal Structure volume 3 issue 11 pages 1225 33 year 1995 month November pmid 8591033 doi url ref The CCP protein itself is structured into two domains, each containing one c type haem group, with a calcium binding site at the domain interface. This family also includes MauG proteins, whose similarity to di haem CCP was previously recognised. ref name pmid9202457 cite journal author Gak ER, Tsygankov YD, Chistoserdov AY title Organization of methylamine utilization genes mau in Methylobacillus flagellatum KT and analysis of mau mutants journal Microbiology Reading, Engl. volume 143 issue 6 pages 1827 35 year 1997 month June pmid 9202457 doi url ref References reflist InterPro content IPR004852 Category Protein ... more details
File F420.png thumb Structure of Coenzyme F sub 420 sub Coenzyme F420 or 8 hydroxy 5 deazaflavin is a coenzyme involved in redox reactions in methanogen s ref cite journal author Deppenmeier U title Redox driven proton translocation in methanogenic Archaea journal Cell. Mol. Life Sci. volume 59 issue 9 pages 1513 33 year 2002 pmid 12440773 doi 10.1007 s00018 002 8526 3 ref , in many Actinobacteria , and sporadically in other bacterial lineages. It is a Flavin group flavin derivative. The coenzyme is a substrate for coenzyme F420 hydrogenase , ref cite journal author Fox JA, Livingston DJ, Orme Johnson WH, Walsh CT date 1987 title 8 Hydroxy 5 deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum 1. Purification and characterization journal Biochemistry. volume 26 pages 4219&ndash 27 pmid 3663585 doi 10.1021 bi00388a007 issue 14 ref 5,10 methylenetetrahydromethanopterin reductase and methylenetetrahydromethanopterin dehydrogenase . ref cite journal author Hagemeier CH, Shima S, Thauer RK, Bourenkov G, Bartunik HD, Ermler U title Coenzyme F420 dependent methylenetetrahydromethanopterin dehydrogenase Mtd from Methanopyrus kandleri a methanogenic enzyme with an unusual quarternary nowiki sic nowiki structure journal J. Mol. Biol. volume 332 issue 5 pages 1047 57 year 2003 pmid 14499608 doi 10.1016 S0022 2836 03 00949 5 ref ref cite journal doi 10.1016 0167 4838 91 90072 8 author GD date 1991 title Purification and properties of 5,10 methylenetetrahydromethanopterin dehydrogenase and 5,10 methylenetetrahydromethanopterin reductase, two coenzyme F420 dependent ... pmid 1911853 last2 Geerts first2 WJ last3 Keltjens first3 JT last4 Van Der Drift first4 C last5 Vogels ... abundance of coenzyme F 420 dependent enzymes in Mycobacterium tuberculosis and other actinobacteria ... 2953692 ref . See also Coenzyme M Coenzyme B Methanofuran Tetrahydromethanopterin References reflist ... cofactors biochem stub Category Coenzymes Category Flavins de F420 fr Coenzyme F420 ja F420 ru ... more details
coenzymeQ sub 10 sub during treatment with HMG CoA reductase inhibitors journal Molecular aspects ... that coenzymeQ sub 10 sub extends the lifespan of C. elegans nematode . ref name pmid 14706236 ...DISPLAYTITLE CoenzymeQ sub 10 sub chembox verifiedrevid 477001960 ImageFile Ubiquinone.png IUPACName ... br Quinone br Plastoquinone CoenzymeQ sub 10 sub , also known as ubiquinone , ubidecarenone , coenzyme ... CoenzymeQ oxidation reduction reactions in mitochondrial electron transport pages 65 82 title Coenzyme ... 122 4 year 1994 pmid 8288904 ref There are three redox states of coenzymeQ sub 10 sub fully oxidized ... CoenzymeQ sub 10 sub was first discovered by Professor Fredrick L. Crane and colleagues at the University ... common CoenzymeQ in human mitochondria is CoQ sub 10 sub . Q refers to the quinone head and 10 ... of CoenzymeQ in Eukaryotes journal Mitochondrion volume 7 issue Suppl pages S62 71 year 2007 month ... cite journal last1 Bhagavan first1 Hemmi N. last2 Chopra first2 Raj K. title CoenzymeQ sub 10 ... in intestinal coenzymeQ sub 10 sub absorption by food intake journal Yakugaku Zasshi volume 127 issue ... be noted that CoQ sub 9 sub is the predominant form of coenzymeQ in rats. ref cite book ... T. last5 Okamoto first6 T. last6 Kishi chapter Metabolism and Exogenous CoenzymeQ sub 10 sub in vivo and Bioavailability of CoenzymeQ sub 10 sub Preparations in Japan title Biomedical and Clinical Aspects of CoenzymeQ pages 131 42 publisher Elsevier location Amsterdam year 1964 ref It appears that CoQ ... Trevisson E, Dimauro S, Navas P, Salviati L title CoenzymeQ deficiency in muscle journal Curr. Opin .... title Safety and tolerability of high dosage coenzymeQ sub 10 sub in Huntington s disease and healthy .... ref cite journal author Hathcock JN, Shao A title Risk assessment for coenzymeQ sub 10 sub Ubiquinone ... author Montero R, S nchez Alc zar JA, Briones P, et al. title Analysis of coenzymeQ sub 10 sub in muscle ... and beta blockers CoenzymeQ sub 10 sub shares a biosynthetic pathway with cholesterol . The synthesis ... more details
?view long&pmid 9782487 doi 10.1099 00221287 144 9 2377 ref chem link coenzyme M CH 3 S CoM HS CoB &rarr chem CH 4 CoB S S CoM This conversion is catalyzed by the enzyme methyl coenzyme M reductase ...chembox Watchedfields changed verifiedrevid 425859719 ImageFile Coenzyme B CoB .svg ImageSize IUPACName 2 7 mercapto 1 oxoheptyl amino 3 phosphonooxybutanoic acid OtherNames Section1 Chembox Identifiers InChI 1 C11H22NO7PS c1 8 19 20 16,17 18 10 11 14 15 12 9 13 6 4 2 3 5 7 21 h8,10,21H,2 7H2,1H3, H,12,13 H,14,15 H2,16,17,18 t8 ,10 m1 s1 InChIKey JBJSVEVEEGOEBZ PSASIEDQBT InChI1 1 C11H22NO7PS c1 8 19 20 16,17 18 10 11 14 15 12 9 13 6 4 2 3 5 7 21 h8,10,21H,2 7H2,1H3, H,12,13 H,14,15 H2,16,17,18 InChIKey1 JBJSVEVEEGOEBZ UHFFFAOYAG SMILES1 O C NC C O O C OP O O O C CCCCCCS StdInChI Ref stdinchicite correct chemspider StdInChI 1S C11H22NO7PS c1 8 19 20 16,17 18 10 11 14 15 12 9 13 6 4 2 3 5 7 21 h8,10,21H,2 7H2,1H3, H,12,13 H,14,15 H2,16,17,18 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey JBJSVEVEEGOEBZ UHFFFAOYSA N CASNo Ref cascite correct ?? CASNo 104302 77 4 PubChem 350 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 343 SMILES O C N C H C O O C H OP O O O C CCCCCCS Section2 Chembox Properties Formula chem C 11 H 22 NO 7 PS MolarMass 343.333641 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Coenzyme B is a coenzyme required for redox reactions in methanogen s. The full chemical name of coenzyme ... ref The molecule contains a thiol , which is its principal site of reaction. Coenzyme B reacts with 2 methylthioethanesulfonate methyl Coenzyme M , abbreviated chem CH 3 S CoM , to release methane ... by fumarate reductase ref cite journal author Heim S, K nkel A, Thauer RK, Hedderich R title Thiol fumarate reductase Tfr from Methanobacterium thermoautotrophicum identification of the catalytic ... fr Coenzyme B gl Coencima B ja B ru B ... more details
1JEX ECnumber Chromosome 18 Arm q Band 23 LocusSupplementaryData Pfam box Symbol Cyt B5 Name Cytochrome ...protein Name Cytochrome b5 caption Rat cytochrome b5 bound to heme image 1jex cyto b5.png width HGNCid ... are water soluble. The family of cytochrome b sub 5 sub like proteins includes besides cytochrome b ... cytochrome b sub 2 sub small L small lactate dehydrogenase EC number 1.1.2.3 , sulfite oxidase EC ... 1.7.1.3 , and plant and fungal cytochrome b sub 5 sub acyl lipid desaturase fusion proteins. Structure 3 D structures of a number of cytochrome b sub 5 sub and yeast flavocytochrome b sub 2 sub are known ... by spatially close N terminal and C terminal segments. The two histidine residues provide the fifth ... crevice. Two isomers of cytochrome b sub 5 sub , referred to as the A major and B minor forms, differ by a 180 rotation of the heme about an axis defined by the and meso carbons. Cytochrome b sub 5 sub in some biochemical reactions EC number 1.6.2.2 cytochrome b5 reductasecytochrome b sub 5 sub reductase NADH H sup sup 2 ferricytochrome b sub 5 sub NAD sup sup 2 ferrocytochrome b sub 5 sub EC number 1.10.2.1 small L small L ascorbate cytochrome b5 reductase ascorbate&mdash cytochrome b sub 5 sub reductase small L small ascorbate ferricytochrome b sub 5 sub monodehydroascorbate ferrocytochrome ... 2 sub O See also P450 containing systems Cytochrome b5, type A References cite journal author Lederer, F. title The cytochrome b sub 5 sub fold an adaptable module journal Biochimie year 1994 volume 76 ..., J.A., Michaelson, L.V. and Sayanova, O. title The role of cytochrome b sub 5 sub fusion desaturases ... 6 issue 2 cite journal author Rivera, M., Barillas Mury, C., Christensen, K.A., Little, J.W., Wells ... studies of the rat outer mitochondrial membrane cytochrome b sub 5 sub journal Biochemistry year 1992 ... Schenkman, J.B. and Jansson, I. title The many roles of cytochrome b sub 5 sub journal Pharmacol ... 2 External links PDB 1B5A Solution structure of rat cytochrome b sub 5 sub form A PDB 1B5B Solution ... more details
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