9 210 Infobox protein family Symbol Cytochrom B C Name CytochromeB C terminal domain image PDB 1bcc ... SMART PROSITE PDOC00171 MEROPS SCOP 1bcc TCDB 3.D.3 OPM family OPM protein CAZy CDD Cytochromeb b6 ... of protein regions in the protonmotive cytochromeb and their possible roles in redox catalysis journal ... T, Meyer A title Mitochondrial cytochromeb evolution and structure of the protein journal ..., cytochromeb is a component of respiratory chain complex III EC number 1.10.2.2 also known as the bc1 ... Cytochromeb b6 ref name PUB00003404 cite journal author Howell N title Evolutionary conservation of protein regions in the protonmotive cytochromeb and their possible roles in redox catalysis journal ... S title Mitochondrial cytochromeb evolution and structure of the protein journal Biochim. Biophys ... and petD genes. Cytochromeb b6 non covalently binds two heme groups, known as b562 and b566 ... groups. Use in phylogenetics Cytochromeb is commonly used to determine phylogenetic relationships ... cite journal last1 Castresana first1 J. title Cytochromeb Phylogeny and the Taxonomy of Great ... in cytochromeb primarily result in exercise intolerance in human patients though more rare ... RW title A mitochondrial cytochromeb mutation causing severe respiratory chain enzyme deficiency ... doi 10.1111 j.1742 4658.2005.04779.x url ref Single point mutations in cytochromeb of Plasdmodium ... 2 Qo 2 of the cytochromeb gene journal Parasitology International volume 57 issue 2 pages 229 32 ... encoding cytochromeb proteins include CYB5A cytochrome b5 type A microsomal CYB5B cytochrome b5 type B outer mitochondrial membrane CYBASC3 cytochromeb, ascorbate dependent 3 MT CYB mitochondrially encoded cytochromeb References reflist External links MeshName Cytochromes b Hemeproteins Category ...Context date October 2009 Pfam box Symbol Cytochrom B N Name image 1l0l opm.gif width 250 caption Mitochondrial cytochrome bc1 complex Pfam PF00033 InterPro IPR005797 SMART PROSITE PDOC00171 SCOP 3bcc ... more details
protein Name cytochromeb reductase 1 caption image width HGNCid 20797 Symbol CYBRD1 AltSymbols DCYTB EntrezGene 79901 OMIM 605745 RefSeq NM 024843 UniProt Q53TN4 PDB ECnumber Chromosome 2 Arm q Band 31 LocusSupplementaryData Duodenal cytochromeB Dcytb has been identified as the reductase enzyme which catalysis catalyzes the reduction of Fe sup 3 sup to Fe sup 2 sup in the process of iron absorption in the duodenum of mammals. ref cite journal author Latunde Dada GO, Van der Westhuizen J, Vulpe CD et al. title Molecular and functional roles of duodenal cytochromeB Dcytb in iron metabolism journal Blood Cells Mol. Dis. volume 29 issue 3 pages 356 60 year 2002 pmid 12547225 doi 10.1006 bcmd.2002.0574 ref According to research carried out, it appears that Dcytb upregulation is controlled by a number of independent stimulators or inhibitors of iron absorption. Furthermore, Dcytb has also been shown to exist in other tissues besides the apical region of the duodenum and as such, it is believed to play a major role in iron metabolism in tissues. References references External links MeshName duodenal cytochromeb, human Iron metabolism Category Physiology Category Enzymes ... more details
, the pyridine hemochrome method. Within each class, cytochrome a , b , or c , early cytochromes are numbered ... and related metabolic pathways class wikitable Cytochromes Combination a and a sub 3 sub Cytochrome c oxidase Complex IV with electrons delivered to complex by soluble cytochrome c hence the name b and Cytochrome C1 c sub 1 sub Coenzyme Q cytochrome c reductase Complex III b sub 6 sub and Cytochrome ...Image Cytochrome c.png thumb 250px Cytochrome c with heme c . Cytochromes are, in general, membrane bound hemoprotein s that contain heme groups and carry out electron transport . They are found either as Protein subunit monomeric protein s e.g., cytochrome c or as Protein subunit subunits of bigger enzymatic complexes that catalyze redox reactions. History Cytochromes were initially described in 1884 by MacMunn as respiratory pigments myohematin or histohematin . ref name MacMunn cite journal doi 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 ... cite journal author Reedy, C. J. & Gibney, B. R. title Heme protein assemblies journal Chem Rev volume ... of flagellum flagella . Types Several kinds of cytochrome exist and can be distinguished by spectroscopy ... types of cytochrome are distinguished by their prosthetic groups class wikitable Type prosthetic group Cytochrome a heme a Cytochromeb heme bCytochrome d tetrapyrrolic chelate of iron ref MeshName Cytochrome d ref The definition of cytochrome c is not defined in terms of the heme group. ref MeshName Cytochrome c Group . ref There is no cytochrome e, but there is a cytochrome f , which is often considered a type of cytochrome c. ref eMedicineDictionary Cytochrome ref In mitochondrion mitochondria ... as the cytochrome P450 oxidase s, so named for the characteristic Soret peak formed by absorbance ... de Cytochrome es Citocromo fa eo Citokromo eu Zitokromo fr Cytochrome id Sitokrom it Citocromi ... 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 The Cytochromeb 245 protein complex is composed of cytochromeb alpha Cytochromeb 245, alpha polypeptide CYBA ref cite web title Entrez Gene CYBA cytochromeb 245, alpha polypeptide url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1535 accessdate ref and beta CYBB ref cite web title Entrez Gene CYBB cytochromeb 245, beta polypeptide chronic granulomatous disease url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1536 accessdate ref chain. Gene expression NOV 002 treatment leads to gene expression changes in SKOV3 cells br CYBA 2.1 fold Cytochromeb 245 ref NOV 002 suppresses tumor cell growth by modulating redox sensitive cell signaling Robert Bowers, Danyelle M. Townsend Christopher J. Pazoles and Kenneth D. Tew Depts. Biomedical and Pharmaceutical Sciences Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina 173 Ashley Ave., Charleston, SC 29425 Novelos Therapeutics, Inc., One Gateway Ctr, Newton, MA 024584 ref alpha polypeptide p22 PHOX br 22 KD subunit of NADPH oxidase br produces superoxide anion br References reflist Category Cytochromes protein stub ... more details
, J.L. title Structural aspects of the cytochromeb sub 6 sub f complex structure of the lumen side domain of cytochrome f journal J. Bioenerg. Biomembr. year 1994 volume 26 pages 31 47 pmid 8027021 doi 10.1007 BF00763218 issue 1 External links PDB 1CTM X ray structure of lumen side domain of cytochrome f from turnip Brassica rapa PDB 1CFM X ray structure of lumen side domain of cytochrome f from Chlamydomonas reinhardtii PDB 1CI3 X ray tructure of soluble domain of cytochrome f from cyanobacterium Phormidium laminosum InterPro IPR002325 InterPro entry for cytochrome f MeshName Cytochrome f InterPro ... JL title The heme redox center of chloroplast cytochrome f is linked to a buried five water chain journal ... JL title The heme redox center of chloroplast cytochrome f is linked to a buried five water chain ... WA, Smith JL title The heme redox center of chloroplast cytochrome f is linked to a buried five water ... The unfinished story of cytochrome f journal Photosynth. Res. year 2004 volume 80 pages 265 276 pmid 16328825 doi 10.1023 B PRES.0000030454.23940.f9 issue 1 3 cite journal author Cramer, W.A., Martinez ... more details
are water soluble. The family of cytochromeb sub 5 sub like proteins includes besides cytochromeb ... cytochromeb 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 cytochromeb sub 5 sub acyl lipid desaturase fusion proteins. Structure 3 D structures of a number of cytochromeb sub 5 sub and yeast flavocytochrome b sub 2 sub are known ... crevice. Two isomers of cytochromeb 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. Cytochromeb sub 5 sub in some biochemical reactions EC number 1.6.2.2 cytochrome b5 reductase cytochromeb 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 cytochromeb sub 5 sub reductase small L small ascorbate ferricytochrome b sub 5 sub monodehydroascorbate ferrocytochrome ..., F. title The cytochromeb 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 cytochromeb sub 5 sub fusion desaturases ... studies of the rat outer mitochondrial membrane cytochromeb sub 5 sub journal Biochemistry year 1992 ... Schenkman, J.B. and Jansson, I. title The many roles of cytochromeb sub 5 sub journal Pharmacol ... 2 External links PDB 1B5A Solution structure of rat cytochromeb sub 5 sub form A PDB 1B5B Solution structure of rat cytochromeb sub 5 sub form B PDB 1CXY X ray structure of cytochromeb sub 558 sub from Ectothiorhodospira vacuolata OMIM 250790 Methemoglobinemia due to deficiency of cytochromeb ...protein Name Cytochrome b5 caption Rat cytochrome b5 bound to heme image 1jex cyto b5.png width HGNCid ... 1JEX ECnumber Chromosome 18 Arm q Band 23 LocusSupplementaryData Pfam box Symbol Cyt B5 Name Cytochrome ... 1x3x , PDB2 2axx , PDB2 2i89 , PDB2 2ibj , PDB2 2oz0 Cytochromes b sub 5 sub are ubiquitous electron ... more details
journal author Passon PG, Hultquist DE title Soluble cytochromeb 5 reductase from human erythrocytes ... cite journal author Michel B, Bosshard HR title Spectroscopic analysis of the interaction between cytochrome ...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 cytochrome c family of proteins. Cytochrome c is a highly soluble protein, unlike other cytochrome s, with a solubility of about 100 g L ... between Coenzyme Q cytochrome c reductase Complexes III Coenzyme Q Cyt C reductase and cytochrome c oxidase IV Cyt C oxidase . In humans, cytochrome c is encoded by the CYCS gene . ref name entrez cite web title Entrez Gene cytochrome c url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ... NO, Hurster KA, Pastorino JG, Schneider T, Russo MA, Farber JL title Cytochrome c release upon ... month March pmid 11790791 doi 10.1074 jbc.M111350200 url ref Function Cytochrome c is a component of the electron transport chain in mitochondria. The heme group of cytochrome c accepts electrons from the b c1 complex and transfers electrons to the cytochrome oxidase complex. Cytochrome c is also involved in initiation of apoptosis . Upon release of cytochrome c to the cytoplasm, the protein binds apoptotic protease activating factor. ref name entrez Cytochrome c can catalyze several reactions ... butyric acid and 4 aminoantipyrine. Species distribution Cytochrome c is a highly conserved protein ... lessons molb.ws.pdf Amino acid sequences in cytochrome c proteins from different species , adapted from Strahler, Arthur Science and Earth History, 1997. page 348. ref The cytochrome c molecule has ... books?id zdeWdF NQhEC&pg PA79&lpg PA79&dq chimpanzee rhesus cytochrome c&source web&ots wbEgDLqBGU&sig ... name indiana Pig s, cow s and sheep also share identical cytochrome c molecules. ref name indiana Classes In 1991 R. P. Ambler recognized four classes of cytochrome c ref name pmid1646017 cite journal ... more details
Pfam box Symbol Cytochrom B559 Name Cytochrome b559, alpha gene psbE and beta gene psbF subunits image PDB 2axt EBI.jpg width caption Structure of Photosystem II from Thermosynechococcus elongatus . ref name pmid16355230 cite journal author Loll B, Kern J, Saenger W, Zouni A, Biesiadka J title Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II journal Nature volume 438 issue 7070 pages 1040 4 year 2005 month December pmid 16355230 doi 10.1038 nature04224 url ref Pfam PF00283 InterPro IPR013081 SMART PROSITE PDOC00464 SCOP TCDB OPM family 2 OPM protein 2axt PDB PDB2 1izl , PDB2 1w5c , PDB2 2axt Pfam box Symbol Cytochrom B559a Name Lumenal portion of Cytochrome b559, alpha gene psbE subunit image PDB 1izl EBI.jpg width caption Structure of oxygen evolving photosystem II from Thermosynechococcus vulcanus . ref name pmid12518057 cite journal author Kamiya N, Shen JR title Crystal structure of oxygen evolving photosystem II from Thermosynechococcus vulcanus at 3.7 A resolution journal Proc. Natl. Acad. Sci. U.S.A. volume 100 issue 1 pages 98 103 year ... , PDB2 2axt Cytochrome b559 is an important component of Photosystem II . PSII is a multisubunit protein ... issue 2 3 pages 75 96 year 2004 pmid 14871485 doi 10.1016 j.bbabio.2003.12.004 ref . Cytochrome b559 ... the haem. Although cytochrome b559 is a redox active protein, it is unlikely to be involved in the primary .... Instead, cytochrome b559 could participate in a secondary electron transport pathway that helps protect PSII from photo damage. Cytochrome b559 is essential for PSII assembly ref name PUB00015364 ... studies of the non heme iron and cytochrome b559 in a Chlamydomonas reinhardtii PSI mutant ... and beta subunits of cytochrome B559. In the alpha sbunit it occurs together with a lumenal domain InterPro IPR013082 , while in the beta subunit it occurs on its own. Cytochrome b559 can exist ... journal author Mizusawa N, Yamashita T, Miyao M title Restoration of the high potential form of cytochrome ... more details
B, de Visser SP, Shaik S title Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes ... 6 deoxyerythronolide B. Cytochrome P450 BM3 CYP102A1 from the soil bacterium Bacillus megaterium ... author R. L. Wright, K. Harris, B. Solow, R. H. White, P. J. Kennelly title Cloning of a potential cytochrome ... CYPs. InterPro subfamilies InterPro subfamilies Cytochrome P450, B class InterPro IPR002397 Cytochrome ...Pfam box Symbol p450 Name Cytochrome P450 image CytP450Oxidase 1OG2.png width caption Cytochrome P450 ... , PDB2 5cpp , PDB2 6cp4 , PDB2 6cpp , PDB2 7cpp , PDB2 8cpp The cytochrome P450 superfamily officially ... title The Ubiquitous Roles of Cytochrome P450 Proteins Metal Ions in Life Sciences edition language ... ref ref name pmid12369887 cite journal author Danielson PB title The cytochrome P450 superfamily ... CytochromeP450.html title Cytochrome P450 Homepage author Nelson D authorlink coauthors ... B o X ane A sub 2 sub S ynthase 1 , and CYP51A1 , lanosterol 14 demethylase, sometimes unofficially ... CytochromeP450.html Cytochrome P450 Homepage and allele names http www.cypalleles.ki.se CYP Allele ... cycle thumb 300px The active site of cytochrome P450 contains a heme iron center. The iron is tethered ... structure of cytochrome P450cam journal J. Mol. Biol. volume 195 issue 3 pages 687 700 year 1987 ..., Paul R. Paul R. Ortiz de Montellano authorlink editor others title Cytochrome P450 structure ... in the electronic state of the active site favors the transfer of an electron from NAD P H via cytochrome ..., Cinti DL, Gibson GG, Schenkman JB title Spin state control of the hepatic cytochrome P450 redox potential ... electron is transferred via the electron transport system, from either cytochrome P450 reductase , ferredoxin s, or cytochrome b5 , reducing the dioxygen adduct to a negatively charged peroxo ... author Rittle J, Green MT title Cytochrome P450 Compound I Capture, Characterization, and C H ..., not mitochondrial CYPs involve the reduction of cytochrome P450 reductase variously CPR, POR, or CYPOR ... more details
Orphan date September 2008 Pfam box Symbol Cytochrom B561 Name Cytochrome b561 image width caption Pfam PF03188 InterPro IPR004877 SMART Prosite SCOP TCDB 5.A.4 OPM family OPM protein PDB Cytochrome b561 is a secretory vesicle specific integral membrane protein responsible for electron transport , binding two heme groups non covalently. Human proteins containing this domain CYB561 CYB561D1 CYB561D2 CYBASC3 CYBRD1 Category Protein domains Category Protein families Category Integral membrane proteins membrane protein stub ... more details
1971 pmid 4993957 doi cite journal author Ozols J title Cytochromeb 5 from a normal human liver ...PBB geneid 1528 Cytochrome b5, form A gene name CYB5A , is a human microsomal cytochrome b5 . ref cite web title Entrez Gene CYB5A Cytochrome b5, form A url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1528 accessdate ref Cytochrome b5 is a membrane bound hemoprotein ..., Millett F title Effect of modification of individual cytochrome c lysines on the reaction with cytochrome ... cite journal author Dailey HA, Strittmatter P title Modification and identification of cytochrome b5 carboxyl groups involved in protein protein interaction with cytochrome b5 reductase. journal ... Mitoma J, Ito A title The carboxy terminal 10 amino acid residues of cytochrome b5 are necessary for its ... and reticulocyte cytochrome b5 mRNAs are products from a single gene. journal Biochem. Biophys. Res ... journal author Shephard EA, Povey S, Spurr NK, Phillips IR title Chromosomal localization of a cytochrome b5 gene to human chromosome 18 and a cytochrome b5 pseudogene to the X chromosome. journal Genomics ... links of the active sites of amidinated cytochrome b5 and NADH cytochrome b5 reductase. journal J ... J title Structure of cytochrome b5 and its topology in the microsomal membrane. journal Biochim. Biophys ... X cite journal author Yoo M, Steggles AW title The complete nucleotide sequence of human liver cytochrome ... Congenital methemoglobinemia with a deficiency of cytochrome b5. journal N. Engl. J. Med. volume 314 ... K, Kimura S, Kizawa R, et al. title Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. journal J. Biochem. volume ... 10.1073 pnas.71.11.4565 pmc 433928 cite journal author Rashid MA, Hagihara B, Kobayashi M, et al. title Structural studies of cytochrome b5. 3. Sequential studies on human liver cytochrome b5. journal ... of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH cytochrome ... more details
, and three are synthesized in the mitochondria. The complex contains two heme s, a cytochrome a and cytochrome a cytochrome a sub 3 sub , and two copper centers, the Cu sub A sub and Cu sub B sub ... bovine heart cytochrome c oxidase at 2.8 A journal Science volume 269 issue 5227 pages 1069 74 year 1995 month August pmid 7652554 doi 10.1126 science.7652554 ref In fact, the cytochrome a sub 3 sub and Cu sub B sub form a binuclear center that is the site of oxygen reduction. Cytochrome c reduced by the preceding component of the respiratory chain cytochrome bc1 complex, complex III docks near the Cu sub A sub binuclear center, passing an electron to it and being oxidized back to cytochrome c containing Fe sup 3 sup . The reduced Cu sub A sub binuclear center now passes an electron on to cytochrome a, which in turn passes an electron on to the cytochrome a sub 3 sub Cu sub B sub binuclear ... bovine enzyme numbering . It plays a vital role in enabling the cytochrome a sub 3 sub Cu sub B sub ... c s, through the Cu sub A sub and cytochrome a sites to the cytochrome a sub 3 sub Cu sub B sub ... the first two electron carriers to the cytochrome a sub 3 sub Cu sub B sub binuclear center, and this electron ... sub B sub sup 2 sup to a water molecule. The fourth electron from another cytochrome c flows through Cu sub A sub and cytochrome a to the cytochrome a sub 3 sub Cu sub B sub binuclear center, reducing ... Cu sub B sub center as it was at the start of this cycle. The net process is that four reduced cytochrome ...enzyme Name Cytochrome c oxidase EC number 1.9.3.1 CAS number 9001 16 5 IUBMB EC number 1 9 3 1 GO code 0009485 image Cytochrome C Oxidase 1OCC in Membrane 2.png width 296px caption The crystal structure of bovine cytochrome c oxidase in a phospholipid bilayer. The intermembrane space lies to top of the image ... transport chain. Complex IV is at the right. The enzyme cytochrome c oxidase or Complex IV PDB ... located in the mitochondrial or bacterial membrane. It receives an electron from each of four cytochrome ... more details
enzyme Name Cytochromeb sub 6 sub f complex EC number 1.10.99.1 image 1q90 opm.gif width 250 caption ... of the lipid bilayer are shown by red and blue dots. The cytochromeb sub 6 sub f complex plastoquinol&mdash ... Complex III of the mitochondria l electron transport chain . For photosynthesis , the cytochromeb ... I . Enzyme structure The cytochromeb sub 6 sub f complex is a dimer, with each monomer composed ... membrane protein cytochromeb 6 f complex from spinach and the cyanobacterium Mastigocladus laminosus ... cytochrome b6 cytochromeb sub 6 sub with a low and high potential heme group, a 19 kDa Rieske protein ... is 217 kDa. The crystal structure of cytochromeb sub 6 sub f complexes from Chlamydomonas reinhardtii ... first4 D. title An atypical haem in the cytochromeb 6 f complex. journal Nature volume 426 issue 6965 ... is structurally similar to cytochrome bc sub 1 sub . Cytochromeb sub 6 sub and subunit IV are homologous to cytochromeb ref name Widger 1984 Cite journal last1 Widger first1 WR. last2 Cramer first2 ... between cytochromeb of mitochondrial complex III and the chloroplast b6 f complex position of the cytochrome ... 105 month Feb year 1994 doi PMID 8081747 ref Cytochromeb sub 6 sub f contains seven prosthetic groups ... in both cytochromeb sub 6 sub f and bc sub 1 sub the c type heme of cytochrome c sub 1 sub and f ... 2S cluster of the Rieske protein. Three unique prosthetic groups are found in cytochromeb sub 6 sub ... function In photosynthesis , the cytochromeb sub 6 sub f complex functions to mediate the transfer ... year 2003 doi 10.1126 science.1090165 PMID 14526088 ref Electron transport via cytochromeb sub 6 ... ATP in chloroplasts. ref name Voet In a separate reaction, the cytochromeb sub 6 sub f complex ... gradient by cytochromeb sub 6 sub f, which can be used to drive ATP synthesis. It has also been ... id accessdate 2011 05 17 doi 10.1016 0005 2728 94 00195 B ref Reaction mechanism The cytochromeb ... align top Q td td align right 2 td tr table ul Cytochromeb sub 6 sub f catalyzes the transfer of electrons ... 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 . Cytochromeb 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 cytochromeb sub 5 sub reductases CYB5R1 CYB5R2 CYB5R3 CYB5R4 See also Cytochrome b5 Methemoglobinemia Reductase External links MeshName CytochromeB 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
Cytochrome c peroxidase , or CCP PDB 2CYP , EC number 1.11.1.5 is a water soluble heme containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c cytochrome c 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 c Cytochrome c 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 Cytochrome c 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 cytochrome c 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 purifies as a consequence of crystallization, making cycles of crystallization an effective final purification step. Much like catalase , the reaction of cytochrome c peroxidase proceeds through a three step process, forming first a CCP compound I and then a CCP compound II CCP ROOH CCP compound I ROH H sub ... kraut projects.html Cytochrome c peroxidase , maintained by the http chem faculty.ucsd.edu ... cytochrome c peroxidase. Peroxidases DEFAULTSORT Cytochrome C Peroxidase Category EC 1.11.1 ... more details
enzyme Name L lactate dehydrogenase cytochrome EC number 1.1.2.3 CAS number 9078 32 4 IUBMB EC number 1 1 2 3 GO code 0004460 image width caption In enzymology , a L lactate dehydrogenase cytochrome EC number 1.1.2.3 is an enzyme that catalysis catalyzes the chemical reaction S lactate 2 ferricytochrome c math rightleftharpoons math pyruvate 2 ferrocytochrome c Thus, the two substrate biochemistry substrates of this enzyme are S lactate and ferricytochrome c , whereas its two product chemistry products are pyruvate and ferrocytochrome c . References reflist Further reading refbegin cite journal author Appleby CA, Morton RK title Lactic dehydrogenase and cytochrome b2 of baker s yeast purification and crystallization journal Biochem. J. volume 71 issue 3 pages 492 9 year 1959 month March pmid 13638255 pmc 1196822 doi url issn cite journal author Appleby CA, Morton RK title Lactic dehydrogenase and cytochrome b2 of baker s yeast. Enzymic and chemical properties of the crystalline enzyme journal Biochem. J. volume 73 issue pages 539 50 year 1959 month November pmid 13793977 pmc 1197094 doi url issn cite journal author Bach SJ, Dixon M, Zerfas LG title Yeast lactic dehydrogenase and cytochromeb 2 journal Biochem. J. volume 40 issue 2 pages 229 39 year 1946 pmid 16747991 pmc 1258326 doi url issn refend 1.1 enzyme stub Alcohol oxidoreductases Category EC 1.1.2 Category Flavin enzymes Category Enzymes of unknown structure ... more details
enzyme Name formate dehydrogenase cytochrome EC number 1.2.2.1 CAS number IUBMB EC number 1 2 2 1 GO code 0047898 image width caption In enzymology , a formate dehydrogenase cytochrome EC number 1.2.2.1 is an enzyme that catalysis catalyzes the chemical reaction formate 2 ferricytochrome b sub 1 sub math rightleftharpoons math CO sub 2 sub 2 ferrocytochrome b sub 1 sub 2 H sup sup Thus, the two substrate biochemistry substrates of this enzyme are formate and ferricytochrome b1 , whereas its 3 product chemistry products are carbon dioxide CO sub 2 sub , ferrocytochrome b1 , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate ferricytochrome b1 oxidoreductase . Other names in common use include formate dehydrogenase , and formate cytochrome b1 oxidoreductase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author Gale EF date 1939 title Formic dehydrogenase of Bacterium coli its inactivation by oxygen and its protection in the bacterial cell journal Biochem. J. volume 33 pages 1012&ndash 1027 1.2 enzyme stub Category EC 1.2.2 Category Enzymes of unknown structure it Formato deidrogenasi citocromo ja ... more details
enzyme Name pyruvate dehydrogenase cytochrome EC number 1.2.2.2 CAS number 9079 84 9 IUBMB EC number 1 2 2 2 GO code 0008985 image width caption In enzymology , a pyruvate dehydrogenase cytochrome EC number 1.2.2.2 is an enzyme that catalysis catalyzes the chemical reaction pyruvate ferricytochrome b sub 1 sub H sub 2 sub O math rightleftharpoons math acetate CO sub 2 sub ferrocytochrome b sub 1 sub The 3 substrate biochemistry substrates of this enzyme are pyruvate , ferricytochrome b1 , and water H sub 2 sub O , whereas its 3 product chemistry products are acetate , carbon dioxide CO sub 2 sub , and ferrocytochrome b1 . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate ferricytochrome b1 oxidoreductase . Other names in common use include pyruvate dehydrogenase , pyruvic dehydrogenase , pyruvic cytochrome b1 dehydrogenase , pyruvate ubiquinone 8 oxidoreductase , and pyruvate oxidase ambiguous . This enzyme participates in pyruvate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Thiamin diphosphate . References reflist 1 cite journal author Williams FR and Hager LP date 1961 title A crystalline flavin pyruvate oxidase journal J. Biol. Chem. volume 236 pages PC36&ndash PC37 cite journal author Koland JG, Gennis RB date 1982 title Identification of an active site cysteine residue in Escherichia coli pyruvate oxidase journal J. Biol. Chem. volume 257 pages 6023&ndash 7 pmid 7042705 issue 11 1.2 enzyme stub Category EC 1.2.2 Category Flavin enzymes Category Thiamin diphosphate enzymes Category Enzymes of unknown structure it Piruvato deidrogenasi citocromo ... more details
enzyme Name cytochrome c 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 Wikify date July 2009 In enzymology , a cytochrome c methionine S methyltransferase EC number 2.1.1.123 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine cytochrome c methionine math rightleftharpoons math S adenosyl L homocysteine cytochrome c S methyl methionine Thus, the two substrate biochemistry substrates of this enzyme are S Adenosyl methionine S adenosyl methionine and cytochrome c methionine , whereas its two product chemistry products are S adenosylhomocysteine and cytochrome c 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 cytochrome c 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 cytochrome c journal J. Biol. Chem. volume 260 pages 537&ndash 45 pmid 2981218 issue 1 DEFAULTSORT Cytochrome C Methionine S Methyltransferase Category EC 2.1.1 Category Enzymes of unknown structure transferase stub it citocromo c metionina S metiltransferasi ... more details
PBB geneid 1535 Cytochromeb 245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis. ref name pmid2243141 cite journal author Dinauer MC, Pierce EA, Bruns GA, Curnutte JT, Orkin SH title Human neutrophil cytochromeb light chain p22 phox . Gene structure, chromosomal location, and mutations in cytochrome negative autosomal recessive chronic granulomatous disease journal J Clin Invest volume 86 issue 5 pages 1729 37 year 1990 month Dec pmid 2243141 pmc 296926 doi 10.1172 JCI114898 ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Cytochromeb is composed of a light chain alpha and a heavy chain beta . This gene encodes ... Gene CYBA cytochromeb 245, alpha polypeptide url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ... mutation in the cytoplasmic domain of the neutrophil p22 phox cytochromeb subunit is associated ... CA, Allen RA, Cochrane CG, Jesaitis AJ title Purified cytochromeb from human granulocyte plasma ... expression of the 22 kilodalton light chain of human neutrophil cytochromeb. journal Proc. Natl ... cite journal author de Boer M, de Klein A, Hossle JP, et al. title Cytochrome b558 negative, autosomal recessive chronic granulomatous disease two new mutations in the cytochrome b558 light chain of the NADPH ... cite journal author Bu Ghanim HN, Casimir CM, Povey S, Segal AW title The alpha subunit of cytochromeb 245 mapped to chromosome 16. journal Genomics volume 8 issue 3 pages 568 70 year 1991 pmid 2286377 ... al. title Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils ... chain of cytochrome b558 of the human NADPH oxidase p22 phox leads to defective translocation ... Y, et al. title Mapping of functional domains in the p22 phox subunit of flavocytochrome b 559 participating ... yes ru b 245, ... more details
enzyme Name D lactate dehydrogenase cytochrome EC number 1.1.2.4 CAS number 37250 79 6 IUBMB EC number 1 1 2 4 GO code 0004458 image width caption In enzymology , a D lactate dehydrogenase cytochrome EC number 1.1.2.4 is an enzyme that catalysis catalyzes the chemical reaction D lactate 2 ferricytochrome c math rightleftharpoons math pyruvate 2 ferrocytochrome c Thus, the two substrate biochemistry substrates of this enzyme are D lactate D lactate and cytochrome c ferricytochrome c , whereas its two product chemistry products are pyruvate and cytochrome c ferrocytochrome c . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is D lactate ferricytochrome c 2 oxidoreductase . Other names in common use include lactic acid dehydrogenase , D lactate cytochrome dehydrogenase , cytochrome dependent D lactate dehydrogenase , D lactate cytochrome c reductase , and D lactic cytochrome c reductase . This enzyme participates in pyruvate metabolism . It employs one cofactor biochemistry cofactor , FAD . This type of enzyme has been characterized in animals, fungi, bacteria and recently in plants ref cite journal url http www.sciencedirect.com science? ob ArticleURL& udi B6T1S 4FV40TJ 1& user 10& rdoc 1& fmt & orig search& sort d& docanchor &view c& acct C000050221& version 1& urlVersion 0& userid 10&md5 5ba860db6f0499628ce76246a7d07d28 author Atlante, A., de Bari, L., Valenti, D., Pizzuto, R., Paventi, G., and Passarella, S. title Transport and metabolism of D lactate in Jerusalem artichoke mitochondria journal Biochim. Biophys. Acta volume 1708 pages 13 22 year 2005 pmid 15949980 doi 10.1016 j.bbabio.2005.03.003 issue 1 ref ref cite journal url http www.jbc.org ... author GREGOLIN C, SINGER TP year 1963 title The lactic dehydrogenase of yeast. III. D Lactic cytochrome ... cytochrome c reductase, a flavoprotein from yeast journal J. Biol. Chem. volume 236 pages 920 ... more details
enzyme Name formate dehydrogenase cytochrome c 553 EC number 1.2.2.3 CAS number IUBMB EC number 1 2 2 3 GO code 0047111 image width caption In enzymology , a formate dehydrogenase cytochrome c 553 EC number 1.2.2.3 is an enzyme that catalysis catalyzes the chemical reaction formate ferricytochrome c 553 math rightleftharpoons math CO sub 2 sub ferrocytochrome c 553 Thus, the two substrate biochemistry substrates of this enzyme are formate and ferricytochrome c 553 , whereas its two product chemistry products are carbon dioxide CO sub 2 sub and ferrocytochrome c 553 . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate ferricytochrome c 553 oxidoreductase . References reflist 1 cite journal author Yagi T date Tokyo title Formate cytochrome oxidoreductase of Desulfovibrio vulgaris journal J. volume Biochem. pages 473&ndash 8 pmid 4982127 issue 4 cite journal author Yagi T date 1979 title Purification and properties of cytochrome c 553, an electron acceptor for formate dehydrogenase of Desulfovibrio vulgaris, Miyazaki journal Biochim. Biophys. Acta. volume 548 pages 96&ndash 105 pmid 226135 issue 1 1.2 enzyme stub Category EC 1.2.2 Category Enzymes of unknown structure it Formato deidrogenasi citocromo c 553 ja c 553 ... more details
enzyme Name glycine dehydrogenase cytochrome EC number 1.4.2.1 CAS number 9075 55 2 IUBMB EC number 1 4 2 1 GO code 0047959 image width caption In enzymology , a glycine dehydrogenase cytochrome EC number 1.4.2.1 is an enzyme that catalysis catalyzes the chemical reaction glycine H sub 2 sub O 2 ferricytochrome c math rightleftharpoons math glyoxylate NH sub 3 sub 2 ferrocytochrome c 2 H sup sup The 3 substrate biochemistry substrates of this enzyme are glycine , water H sub 2 sub O , and ferricytochrome c , whereas its 4 product chemistry products are glyoxylate , ammonia NH sub 3 sub , ferrocytochrome c , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH2 group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is glycine ferricytochrome c oxidoreductase deaminating . This enzyme is also called glycine cytochrome c reductase . This enzyme participates in glycine, serine and threonine metabolism . References reflist 1 cite journal author Sanders HK, Becker GE, Nason A date 1972 title Glycine cytochrome c reductase from Nitrobacter agilis journal J. Biol. Chem. volume 247 pages 2015&ndash 25 pmid 5016640 issue 7 1.4 enzyme stub Category EC 1.4.2 Category Enzymes of unknown structure it Glicina deidrogenasi citocromo ja ... more details
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