Pfam box Symbol COX3 Name CytochromecoxidasesubunitIII image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromecoxidase. ref name pmid15299438 cite journal author Miki ... 273 PDB3 1fft H 1 203 CytochromecoxidasesubunitIII is one of main transmembrane subunits of cytochromecoxidaseCytochromecoxidase EC number 1.9.3.1 is the terminal enzyme of the respiratory chain ... cytochromecoxidase contains three common subunits, Cytochromecoxidasesubunit I I , Cytochromecoxidasesubunit II II and III . In prokaryotes, subunits I and III can be fused and a fourth subunit ... three core subunits Cytochromecoxidasesubunit I subunit I is the most conserved subunit, whereas Cytochromecoxidasesubunit II subunit II is the least conserved ref name PUB00006601 cite journal ... 8083153 pmc 196760 ref . Subfamilies Cytochrome o ubiquinol oxidase, subunitIII InterPro IPR014206 Cytochrome aa3 quinol oxidase, subunitIII InterPro IPR014246 Examples Human genes encoding proteins ... subunit oxidized cytochromecoxidase at 2.8 A. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi ... Michel H title Cytochromecoxidase catalytic cycle and mechanisms of proton pumping a discussion ... coupled electron transfer drives the proton pump of cytochromecoxidase journal Nature volume 440 issue 7085 pages 829 32 year 2006 pmid 16598262 doi 10.1038 nature04619 ref . Cytochromecoxidase ... the cytochromec but the quinol ubiquinol oxidation they belong to the same haem copper oxidase ... oxidase of Escherichia coli and the aa3 type family of cytochromec oxidases journal J. Biol. Chem ... 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 ... of the deduced primary structures for subunits I and III of cytochrome caa3 journal J. Biol. Chem. volume ... are branched, they have a number of distinct terminal oxidases, rather than the single cytochromec ... more details
Orphan date February 2009 Pfam box Symbol COX5B Name Cytochromecoxidasesubunit Vb image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromecoxidase. 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 Cytochromecoxidase, subunit Vb is a subunit of mitochondrial cytochromecoxidase complex. Cytochromecoxidase 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 cytochromecoxidase journal Biochim. Biophys. Acta volume 726 issue 2 pages 135 148 year 1983 pmid 6307356 ref In eukaryotes ... of the 13 subunit oxidized cytochromecoxidase at 2.8 A journal Science volume 272 issue 5265 ...?PDOC00663 Cytochromecoxidasesubunit 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 cytochromecoxidase 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 ... in the plasma membrane. In eukaryotes, in addition to the three large subunits, I, II and III, that form ... and IV in yeast, binds a zinc atom. The sequence of subunit Vb is well conserved and includes three ... more details
Pfam box Symbol COX2 TM Name Cytochromecoxidasesubunit II, transmembrane domain image 1qle opm.gif width 250 caption Bacterial cytochromecoxidase 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 CytochromeCoxidasesubunit II, periplasmic domain image width caption Pfam PF00116 InterPro IPR002429 ... 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 Cytochromecoxidasesubunit II , abbreviated CoxII , is the second subunit of cytochromecoxidase . Cytochromecoxidase EC number 1.9.3.1 ref name PUB00000581 cite journal author Capaldi RA, Malatesta F, Darley Usmar VM title Structure of cytochromecoxidase journal ... polypeptides mammals . In Leigh s disease , there may be an abnormality or deficiency of cytochromeoxidase. Subunit 2 CO II transfers the electrons from cytochromec to the Main subunit of cytochromecoxidase catalytic subunit 1 . It contains two adjacent transmembrane regions in its N terminus and the major ... Cu A see InterPro IPR001505 , probably the primary acceptor in cytochromecoxidase. An exception is the corresponding subunit of the cbb3 type oxidase which lacks the copper A redox centre. Several bacterial CO II have a C terminal extension that contains a covalently bound haem c. The N terminal domain of cytochromeCoxidase contains two transmembrane alpha helices. Human proteins containing this domain COII COX2 MT CO2 References reflist Further Reading The whole structure of the 13 subunit oxidized cytochromecoxidase at 2.8 A. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H ... chain and is involved in the transfer of electrons from cytochromec to oxygen. In eukaryotes ... more details
1ehk A 218 309 PDB3 1fft A 47 505 PDB3 1xme A 18 108 CytochromeC and Quinol oxidase polypeptide I is main subunit of cytochromecoxidase complex. Cytochromecoxidase EC number 1.9.3.1 is a key enzyme ... methosulphate can act as acceptor. Subfamilies Cytochromecoxidase cbb3 type, subunit I InterPro IPR004677 Cytochrome o ubiquinol oxidase, subunit I InterPro IPR014207 Cytochrome aa3 quinol oxidase, subunit I InterPro IPR014233 Cytochromecoxidase, subunit I bacterial type InterPro IPR014241 Examples In humans, the main subunit of cytochromecoxidase is encoded by the MT CO1 gene. References ...Pfam box Symbol COX1 Name CytochromeC and Quinol oxidase polypeptide I image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromecoxidase. ref name pmid8638158 cite journal author Tsukihara T, Aoyama H, Yamashita E, et al. title The whole structure of the 13 subunit oxidized cytochromecoxidase at 2.8 A journal Science volume 272 issue 5265 pages 1136 44 year 1996 month ..., 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 cytochromecoxidase journal Biochim ... quinol oxidase was derived from cytochromecoxidase in Gram positive bacteria and that archaebacterial quinol oxidase has an independent origin. A considerable amount of evidence suggests that proteobacteria Purple bacteria acquired quinol oxidase through a lateral gene transfer from ... mammals of which only the catalytic subunit equivalent to mammalian subunit I CO I is found ... cite journal author Saraste M, Castresana J, Higgins DG, Lubben M title Evolution of cytochromeoxidase, an enzyme older than atmospheric oxygen journal EMBO J. volume 13 issue 11 pages 2516 2525 ... cite journal author Saraste M, Holm L, Wikstrom M title Structural models of the redox centres in cytochromeoxidase journal EMBO J. volume 6 issue 9 pages 2819 2823 year 1987 pmid 2824194 pmc 553708 ... more details
See also Cytochromecoxidasesubunit I Cytochromecoxidasesubunit II Cytochromecoxidasesubunit ...enzyme Name Cytochromecoxidase EC number 1.9.3.1 CAS number 9001 16 5 IUBMB EC number 1 9 3 1 GO code 0009485 image CytochromeCOxidase 1OCC in Membrane 2.png width 296px caption The crystal structure of bovine cytochromecoxidase in a phospholipid bilayer. The intermembrane space lies to top of the image ... transport chain. Complex IV is at the right. The enzyme cytochromecoxidase or Complex IV PDB ... bovine heart cytochromecoxidase at 2.8 A journal Science volume 269 issue 5227 pages 1069 ... ion in the fully oxidized state. X ray crystallography Crystallographic studies of cytochromecoxidase ... Biogenesis of cytochromecoxidase journal Mitochondrion volume 5 issue 6 pages 363 88 year 2005 month ... Fontanesi F, Soto IC, Horn D, Barrientos A title Assembly of mitochondrial cytochromecoxidase ... cytochromecoxidase of human mitochondrial respiratory chain journal Pharmacol. Toxicol. volume ... ref all bind to cytochromecoxidase, thus competitive inhibition competitively inhibiting the protein ... defects and disorders Defects involving genetic mutations altering cytochromecoxidase COX functionality ... H, Hans kov H, Zeman J, Houstek J title Genetic defects of cytochromecoxidase assembly journal ... model of cytochromecoxidase Requires http www.mdl.com products framework chime MDL Chime UMichOPM families superfamily 4 MeshName CytochromecOxidase Electron transport chain Proton pumps Mitochondrial DNA DEFAULTSORT CytochromeCOxidase Category Cellular respiration Category EC 1.9.3 Category ... Cytochrom cOxidase es Citocromo c oxidasa fa fr Cytochromec oxydase id Sitokrom ... 3 sub and Cu sub B sub form a binuclear center that is the site of oxygen reduction. Cytochromec reduced by the preceding component of the respiratory chain cytochrome bc1 complex, complex III docks ... c containing Fe sup 3 sup . The reduced Cu sub A sub binuclear center now passes an electron on to cytochrome ... more details
between Coenzyme Q cytochromec reductase Complexes III Coenzyme Q Cyt C reductase and cytochromecoxidase IV Cyt Coxidase . 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 ... c and cytochromecoxidase journal J. Biol. Chem. volume 259 issue 16 pages 10085 91 publisher ... first V authorlink coauthors Alleyne T year 2001 month Dec. title Cytochromeccytochromecoxidase ... of cytochrome a in cytochromecoxidase journal J. Biol. Chem. volume 267 issue 1 pages 298 302 publisher ... affects the conformation of cytochrome a in cytochromecoxidase journal J. Biol. Chem. volume 267 ... of cytochromec with cytochromecoxidase an understanding of the high to low affinity transition ... between cytochromec and cytochromecoxidase journal J. Biol. Chem. volume 259 issue 16 pages ... c with cytochrome c1 and cytochromeoxidase journal J. Biol. Chem. volume 256 issue 10 pages 4984 ...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 cytochromeoxidase 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 ... more details
OPM protein CAZy CDD Infobox protein family Symbol Cytochrom CIII Name Class IIIcytochromeC family ...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 ... 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
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
H title Mutant and wild type alpha synuclein interact with mitochondrial cytochromeCoxidase journal ... width caption coproporphyrinogen iiioxidase from leishmania major Pfam PF01218 Pfam clan InterPro ... IIIoxidase, mitochondrial is an enzyme that in humans is encoded by the CPOX gene . ref name ... Y title A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant ... T, Yoshinaga T, Tokunaga R, Taketani S title Coproporphyrinogen oxidase. Purification, molecular ... Entrez Gene CPOX coproporphyrinogen oxidase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ... of coproporphyrinogen III to Protoporphyrinogen IX proto porphyrinogen IX in the haem and chlorophyll ... T, Tokunaga R, Taketani S title Coproporphyrinogen oxidase. Purification, molecular cloning, and induction ... Madsen O, Sandal L, Sandal NN, Marcker KA title A soybean coproporphyrinogen oxidase gene is highly ... JM, Chambon H, Jolles J, Labbe P title Purification and properties of coproporphyrinogen oxidase from ... and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria ... of the human coproporphyrinogen oxidase gene to chromosome band 3q12 journal Hum. Genet ... Larue MH, Martasek P, Grandchamp B title Coproporphyrinogen oxidase gene organization and description ... oxidase and common intragenic polymorphisms journal Hum. Mol. Genet. volume 3 issue ... expression of a cDNA encoding human coproporphyrinogen oxidase journal Proc. Natl. Acad. Sci. U.S.A. ... coproporphyrinogen oxidase journal Biochim. Biophys. Acta volume 1183 issue 3 pages 547 9 year 1994 ... J title Three novel mutations in the coproporphyrinogen oxidase gene journal Hum. Mutat. volume 9 ... 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria journal ... novel mutations in the coproporphyrinogen oxidase gene journal Hum. Mutat. volume 10 issue 3 pages ... first6 Hideo cite journal author Rosipal R title Systematic analysis of coproporphyrinogen oxidase ... more details
enzyme Name iron cytochromec 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 cytochromec 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 cytochromec 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 cytochromec 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 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
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
Pfam box Symbol ATP synt C Name image 2bl2.gif width 250 caption V type sodium ATPase from Enterococcus hirae . Calculated hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots Pfam PF00137 InterPro IPR002379 SMART Prosite PDOC00526 SCOP 1aty TCDB OPM family 5 OPM protein 2bl2 PDB PDB3 2bl2 C 14 79 PDB3 1yce S 13 81 PDB3 1wu0 A 3 72 PDB3 1c17 D 8 77 PDB3 1j7f D 8 77 PDB3 1c99 A 8 77 PDB3 1a91 8 77 PDB3 1l6t A 8 77 PDB3 1c0v A 8 77 PDB3 1aty 9 77 PDB3 1ijp A 8 77 ATPase, subunitC of F0 V0 complex is the main transmembrane subunit of V type , A type and F type ATP synthase s. ATPases or ATP synthases are membrane bound enzyme complexes ion transporters that combine ATP synthesis and or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... ref . SubunitC also called subunit 9, or proteolipid in F ATPases, or the 16 kDa ... that subunitC of the V ATPase is in close proximity to subunits E and G of the V1 domain and subunit ... ATPase, V0 complex, proteolipid subunitC , InterPro IPR000245 ATPase, F0 complex, subunitC InterPro ... reflist InterPro content DEFAULTSORT Atp Synthase SubunitC Category Protein domains Category Protein ..., ten C subunits form an oligomeric ring that makes up the F0 rotor. The flux of protons through the ATPase channel drives the rotation of the Csubunit ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the Csubunit ring of F0. The sequential protonation and deprotonation of Asp61 of subunitC is coupled to the stepwise movement of the rotor ref name PUB00020632 cite journal author Fillingame RH, Angevine CM, Dmitriev OY title Mechanics of coupling proton movements to c ring ... 10.1016 S0014 5793 03 01101 3 ref . In V ATPases, there are three proteolipid subunits c, c and c ... more details
and related metabolic pathways class wikitable Cytochromes Combination a and a sub 3 sub Cytochromecoxidase Complex IV with electrons delivered to complex by soluble cytochromec hence the name b and Cytochrome C1 c sub 1 sub Coenzyme Q cytochromec reductase Complex III b sub 6 sub and Cytochrome ...Image Cytochrome c.png thumb 250px Cytochromec 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., 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 ... as the cytochrome P450 oxidase s, so named for the characteristic Soret peak formed by absorbance ... 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 ... de Cytochrome es Citocromo eo Citokromo eu Zitokromo fa fr Cytochrome id Sitokrom it Citocromi ... more details
illustration of complex III reactions The coenzyme Q cytochromec oxidoreductase , sometimes called the cytochrome bc sub 1 sub complex , and at other times complex III , is the third complex in the electron ... L sub and b sub H sub , the cytochromecsubunit has one c type heme Cytochrome C1 c sub 1 sub , and the Rieske ... of complex III PDB 1KYO , PDB 1L0L Reaction It catalyzes the reduction of Cytochromeccytochrome ... matrix to the intermembrane space QH sub 2 sub 2 cytochromec Fe sup III sup 2 H sup sup sub ... CAZy CDD enzyme Name ubiquinol cytochromec reductase EC number 1.10.2.2 CAS number 9027 03 6 IUBMB ... the mitochondrial cytochrome b and the nuclear genomes all other subunits . Complex III is present ... complex chemistry complex contains 11 subunits, 3 respiratory protein subunit subunits cytochrome B ... cytochromec reductase catalyzes the chemical reaction QH sub 2 sub 2 ferricytochrome c math ... 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 ... ferricytochrome c oxidoreductase . Other names in common use include coenzyme Q cytochromec reductase, dihydrocoenzyme Q cytochromec reductase, reduced ubiquinone cytochromec reductase, complex III, mitochondrial electron transport , ubiquinone cytochromec reductase, ubiquinol cytochromec oxidoreductase, reduced coenzyme Q cytochromec reductase, 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 cytochromec reductase, and QH2 cytochromec oxidoreductase. Structure Image Cytochrome bc1 complex.png thumb 400px Structure of complex III Compared to the other ... more details
E, Kim S, Paik WK year 1977 title Cytochromec specific protein methylase III from Neurospora crassa ...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 ... 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
enzyme Name trimethylamine N oxide reductase cytochromec 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 reductase cytochromec EC number 1.7.2.3 is an enzyme that catalysis catalyzes the chemical reaction trimethylamine 2 ferricytochrome csubunit H sub 2 sub O math rightleftharpoons math trimethylamine N oxide 2 ferrocytochrome csubunit 2 H sup sup The 3 substrate biochemistry substrates of this enzyme are trimethylamine , ferricytochrome csubunit , and water H sub 2 sub O , whereas its 3 product chemistry products are trimethylamine N oxide , ferrocytochrome csubunit , 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 journal Biol. Chem. volume 378 pages 293&ndash 302 pmid 9165084 issue 3 4 cite journal author Czjzek ... 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 ... reduttasi citocromo c ja N c ... 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
An oxidase is any enzyme that catalyst catalyzes an redox oxidation reduction reaction involving molecular oxygen O sub 2 sub as the electron acceptor. In these reactions, oxygen is reduced to water H sub 2 sub O or hydrogen peroxide H sub 2 sub O sub 2 sub . The oxidases are a subclass of the oxidoreductase s. Examples An important example is cytochromecoxidase , the key enzyme that allows the body to employ oxygen in the generation of energy and the final component of the electron transfer chain . Other examples are glucose oxidase monoamine oxidasecytochrome P450 oxidase NADPH oxidase Xanthine oxidase L gulonolactone oxidase laccase lysyl oxidaseOxidase test main Oxidase test In microbiology , the oxidase test is used as a Phenotype phenotypic characteristic for the identification of bacteria l strains it determines whether a given bacterium produces cytochrome oxidases and therefore utilizes oxygen with an electron transfer chain . External links Catalase & Oxidase tests http www.tgw1916.net movies.html video MeshName Oxidase Enzymes Category Oxidoreductases ar ca Oxidasa et Oks daas es Oxidasa eu Oxidasa fr Oxydase io Oxidazo nl Oxidase ja pl Oksydazy pt Oxidase sv Oxidaser uk ... 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
PBB geneid 6391 Succinate dehydrogenase complex subunitC , also known as succinate dehydrogenase cytochrome b560 subunit, mitochondrial , is a protein that in humans is encoded by the SDHC gene . ref name entrez cite web title Entrez Gene succinate dehydrogenase complex url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 6391 accessdate ref ref name pmid9533030 cite journal author Hirawake H, Taniwaki M, Tamura A, Kojima S, Kita K title Cytochrome b in human complex II succinate ubiquinone oxidoreductase cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large SDHC and small SDHD subunits to 1q21 and 11q23 journal Cytogenet. Cell Genet. volume 79 issue 1 2 pages 132 8 year 1997 pmid 9533030 doi 10.1159 000134700 url issn ref Gene The gene that codes for the SDHC protein is nuclear, even though the protein is located in the inner membrane of the mitochondria . The location of the gene in humans is on the Chromosome 1 human first chromosome at q21. The gene is partitioned in 6 exon s. The expressed protein has 170 amino acids. Function File SuccDeh.svg thumb left The SDHC protein one of four nuclear encoded ... Interactive pathway map TCACycle WP78 highlight Succinate dehydrogenase complex subunitC References ... enzymes DEFAULTSORT Succinate Dehydrogenase Complex SubunitC Category Genes Category EC 1.3.5 Biochem ... . The SDHA subunit is connected to the SDHB subunit on the hydrophilic, catalytic end of the complex ... sub 2 sub . Electrons from the FADH sub 2 sub are transferred to the SDHB subunit iron clusters 2Fe ... Ricketts C, Woodward ER, Killick P, et al. title Germline SDHB mutations and familial renal cell ... 1054 6 year 2007 pmid 17804857 doi 10.1056 NEJMc071191 cite journal author Eng C, Kiuru M, Fernandez ... pmid 19768395 doi 10.1007 s10286 009 0028 z cite journal author Pigny P, Cardot Bauters C, Do Cao C, et al. title Should genetic testing be performed in each patient with sporadic pheochromocytoma ... more details
A subunit is a subdivision of a larger unit . In military organizations, a sub unit is smaller in size than a battalion and is commanded by an Officer Commanding . In chemistry, the term can refer to a monomer . In biochemistry, it may apply to the protein subunit s. wiktionary subunit disambig vi Ti u n v ... 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
Infobox protein family Symbol FAD oxidaseC Name FAD linked oxidases, C terminal domain image PDB 1wve EBI.jpg width caption p cresol methylhydroxylase alteration of the structure of the flavoprotein subunit upon its binding to the cytochromesubunit Pfam PF02913 Pfam clan CL0277 InterPro IPR004113 SMART PROSITE MEROPS SCOP 1ahu TCDB OPM family OPM protein CAZy CDD In molecular biology FAD oxidases are a family of FAD dependent oxidoreductases . They are flavoprotein s that contain a covalently bound FAD group which is attached to a histidine via an 8 alpha N3 histidyl riboflavin linkage. The region around the histidine that binds the FAD group is conserved sequence conserved in these enzyme s. ref name pmid9141139 Cite pmid 9141139 ref References reflist InterPro content IPR004113 Category Protein domains ... more details
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