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 on Myohaematin and the Histohaematins journal Philosophical Transactions of the Royal Society of London volume 177 publisher The Royal Society year 1886 ref In the 1920s, Keilin rediscovered these respiratory ..., the pyridine hemochrome method. Within each class, cytochrome a , b , or c , early cytochromes are numbered ... 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 Cytochrome b heme b Cytochrome 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 ... 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 ... 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
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 Cytochrome b 245 protein complex is composed of cytochrome b alpha Cytochrome b 245, alpha polypeptide CYBA ref cite web title Entrez Gene CYBA cytochrome b 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 cytochrome b 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 Cytochrome b 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
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 ... X url ref Class I includes the lowspin soluble cytochrome c of mitochondria and bacteria. It has the heme ... residue towards the C terminus. Class II includes the highspin cytochrome c . It has the heme attachment ... more details
cytochrome bc1 complex Pfam PF00033 InterPro IPR005797 SMART PROSITE PDOC00171 SCOP 3bcc ... 9 210 Infobox protein family Symbol Cytochrom B C Name Cytochrome B C terminal domain image PDB 1bcc EBI.jpg width caption cytochrome bc1 complex from chicken Pfam PF00032 Pfam clan InterPro IPR005798 SMART PROSITE PDOC00171 MEROPS SCOP 1bcc TCDB 3.D.3 OPM family OPM protein CAZy CDD Cytochrome b b6 is the main subunit of transmembrane cytochrome bc1 complex cytochrome bc1 and Cytochrome b6f complex ... of protein regions in the protonmotive cytochrome b and their possible roles in redox catalysis journal ... T, Meyer A title Mitochondrial cytochrome b evolution and structure of the protein journal ..., cytochrome b is a component of respiratory chain complex III EC number 1.10.2.2 also known as the bc1 complex or ubiquinol cytochrome c reductase. In plant chloroplasts and cyanobacteria, there is an analogous protein, cytochrome b6, a component of the plastoquinone plastocyanin reductase EC ... Cytochrome b b6 ref name PUB00003404 cite journal author Howell N title Evolutionary conservation of protein regions in the protonmotive cytochrome b and their possible roles in redox catalysis journal ... S title Mitochondrial cytochrome b evolution and structure of the protein journal Biochim. Biophys ... segments. In plants and cyanobacteria, cytochrome b6 consists of two subunits encoded by the petB and petD genes. Cytochrome b b6 non covalently binds two heme groups, known as b562 and b566 ... groups. Use in phylogenetics Cytochrome b is commonly used to determine phylogenetic relationships ... relationships within Family biology families and Genus genera . Comparative studies involving cytochrome ... cite journal last1 Castresana first1 J. title Cytochrome b Phylogeny and the Taxonomy of Great ... in cytochrome b primarily result in exercise intolerance in human patients though more rare ... RW title A mitochondrial cytochrome b mutation causing severe respiratory chain enzyme deficiency ... more details
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 ..., J.L. title Structural aspects of the cytochrome b 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 ... more details
protein Name Cytochrome b5 caption Rat cytochrome b5 bound to heme image 1jex cyto b5.png width HGNCid 2570 Symbol CYB5A AltSymbols CYB5 EntrezGene 1528 OMIM 250790 RefSeq NM 001914 UniProt P00167 PDB 1JEX ECnumber Chromosome 18 Arm q Band 23 LocusSupplementaryData Pfam box Symbol Cyt B5 Name Cytochrome b5 Pfam PF00173 InterPro IPR001199 PROSITE PDOC00170 PDB PDB2 1aqa , PDB2 1aw3 , PDB2 1awp , PDB2 ... 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 ... 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 reductase cytochrome b sub 5 sub ... EC number 1.10.2.1 small L small L ascorbate cytochrome b5 reductase ascorbate&mdash cytochrome b sub ... 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 ... 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 structure of rat cytochrome b sub 5 sub form B PDB 1CXY X ray structure of cytochrome b sub 558 sub from Ectothiorhodospira vacuolata OMIM 250790 Methemoglobinemia due to deficiency of cytochrome b ... 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
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
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 ... 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 ... B, de Visser SP, Shaik S title Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes ... 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 by NADPH , and the transfer of reducing power as electrons to the CYP. Cytochrome b5 cyb5 can also contribute reducing power to this system after being reduced by cytochrome b5 reductase CYB5R ... systems in which both electrons required by the CYP come from cytochrome b5 . FMN Fd P450 systems originally ... account for their central importance in medicine . Cytochrome P450 enzymes are present in most tissues ... 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 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
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 ..., 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 ... ion in the fully oxidized state. X ray crystallography Crystallographic studies of cytochrome c oxidase ... bovine enzyme numbering . It plays a vital role in enabling the cytochrome a sub 3 sub Cu sub B sub ... Biogenesis of cytochrome c 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 cytochrome c oxidase ... Biochemistry Summary reaction 4 Fe sup 2 sup cytochrome c 8 H sup sup sub in sub O sub 2 sub 4 Fe sup 3 sup cytochrome c 2 H sub 2 sub O 4 H sup sup sub out sub Two electrons are passed from two cytochrome ... more details
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 ... Structural studies of cytochrome b5. 3. Sequential studies on human liver cytochrome b5. journal ... 1971 pmid 4993957 doi cite journal author Ozols J title Cytochrome b 5 from a normal human liver ... of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH cytochrome ... outer membrane isoform of cytochrome b5 is contained within the carboxyl terminal region ... 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
protein Name cytochrome b 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 cytochrome B 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 cytochrome B 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 cytochrome b, human Iron metabolism Category Physiology Category Enzymes ... more details
enzyme Name iron cytochrome c reductase 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 cytochrome c reductase 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 cytochrome c reductase . 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 cytochrome c reductase 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 cytochrome c 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 Cytochrome c peroxidase , or CCP 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 ... faculty.ucsd.edu kraut projects.html Cytochrome c peroxidase , maintained by the http chem faculty.ucsd.edu ... entry for yeast cytochrome c peroxidase. Peroxidases DEFAULTSORT Cytochrome C Peroxidase Category EC ... 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 Cytochrome b sub 6 sub f complex EC number 1.10.99.1 image 1q90 opm.gif width 250 caption Crystal structure of the cytochrome b6f complex from C. reinhardtii PDB3 1q90 . Hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots. The cytochrome b sub 6 sub f complex plastoquinol&mdash ... The reaction is analogous to the reaction catalyzed by cytochrome bc1 complex cytochrome bc sub 1 sub Complex III of the mitochondria l electron transport chain . For photosynthesis , the cytochrome b ... I . Enzyme structure The cytochrome b sub 6 sub f complex is a dimer, with each monomer composed ... membrane protein cytochrome b 6 f complex from spinach and the cyanobacterium Mastigocladus laminosus ... ref These consist of four large subunits a 32 kDa cytochrome f with a c type cytochrome, a 25 kDa cytochrome b6 cytochrome b sub 6 sub with a low and high potential heme group, a 19 kDa Rieske protein ... is 217 kDa. The crystal structure of cytochrome b sub 6 sub f complexes from Chlamydomonas reinhardtii ... first4 D. title An atypical haem in the cytochrome b 6 f complex. journal Nature volume 426 issue 6965 ... of the cytochrome b6f complex quinone analogue inhibitors as ligands of heme cn. journal J Mol Biol ... Cytochrome b6f Complex from Nostoc sp. PCC 7120. journal J Biol Chem volume 284 ... is structurally similar to cytochrome bc sub 1 sub . Cytochrome b sub 6 sub and subunit IV are homologous to cytochrome b ref name Widger 1984 Cite journal last1 Widger first1 WR. last2 Cramer first2 ... between cytochrome b of mitochondrial complex III and the chloroplast b6 f complex position of the cytochrome ... However, cytochrome f and cytochrome C1 cytochrome c sub 1 sub are not homologous. ref name Martinez ... Cramer first4 WA. last5 Smith first5 JL. title Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. journal Structure volume 2 issue 2 pages 95 105 month Feb year 1994 doi PMID 8081747 ref Cytochrome b sub 6 sub f contains seven prosthetic groups ... 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 cytochrome b 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 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
enzyme Name Cytochrome c 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 cytochrome c 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 cytochrome c 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 Cytochrome c 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 cytochrome c nitrite reductase NrfA journal Meth. Enzymol. volume 437 issue pages 63 77 year 2008 pmid 18433623 doi 10.1016 S0076 6879 07 37004 3 ref The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during wikt anaerobic anaerobic conditions. During ... 10.1111 j.1574 6976.2002.tb00616.x ref Cytochrome c Nitrite Reductase is a homodimer which contains ..., Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM title Structure of cytochrome ... on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme ... GP, Bartunik HD, Huber R, Kroneck PM title Structure of cytochrome c nitrite reductase journal ... 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
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