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 ... between Coenzyme Q cytochromec reductase Complexes III and cytochromec oxidase IV . In humans, cytochromec is encoded by the CYCS gene . ref name entrez cite web title Entrez Gene cytochrome ... T, Russo MA, Farber JL title Cytochromec release upon Fas receptor activation depends on translocation ... jbc.M111350200 url issn ref Function Cytochromec is a component of the electron transport chain in mitochondria. The heme group of cytochromec accepts electrons from the b c1 complex and transfers electrons to the cytochrome oxidase complex. Cytochromec is also involved in initiation of apoptosis . Upon release of cytochromec to the cytoplasm, the protein binds apoptotic protease activating factor. ref name entrez Cytochromec can catalyze several reactions such as hydroxylation and aromatic .... Species distribution Cytochromec is a highly conserved protein across the spectrum of species ... in cytochromec proteins from different species , adapted from Strahler, Arthur Science and Earth History, 1997. page 348. ref The cytochromec molecule has been studied for the glimpse it gives ... also share identical cytochromec molecules. ref name indiana Classes In 1991 R. P. Ambler recognized four classes of cytochromec ref name pmid1646017 cite journal author Ambler RP title Sequence variability ... soluble cytochromec of mitochondria and bacteria. It has the heme attachment site towards the N .... Class II includes the highspin cytochromec . It has the heme attachment site closed to the N terminus ... prosthetic groups as well as heme c. Applications Cytochromec is suspected to be the functional complex ... of increasing activity of cytochromec , thus increasing metabolic activity and freeing up more ... 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 Wikify date July 2009 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
Image ETC.PNG thumb 300px Electron transport chain. Complex IV is at the right. Image CytochromeC Oxidase 1OCC in Membrane 2.png thumb 300px The crystal structure of bovine cytochromec oxidase in a phospholipid ... dimer in this structure The enzyme cytochromec oxidase or Complex IV PDB 2OCC , EC number 1.9.3.1 ... or bacterial membrane. It receives an electron from each of four cytochromec molecules, and transfers ... Cytochromec Oxidase at 2.8 journal Science volume 269 issue 5227 pages 1069 1074 doi 10.1126 science.7652554 ... c reduced by the preceding component of the respiratory chain cytochrome bc1 complex, complex III ... Biogenesis of Cytochromec Oxidase journal Mitochondrion volume 5 issue 6 pages 363 383 url doi 10.1016 ..., A. year 2006 title Assembly of mitochondrial cytochromec oxidase, a complicated and highly ... cytochromec 8 H sup sup sub in sub O sub 2 sub 4 Fe sup 3 sup cytochromec 2 H sub 2 sub O 4 H sup sup sub out sub Two electrons are passed from two cytochromec s, through the Cu sub A sub and cytochrome ... electron arising from another cytochromec is passed through the first two electron carriers to the cytochrome .... The fourth electron from another cytochromec flows through Cu sub A sub and cytochrome a to the cytochrome .... The net process is that four reduced cytochromec s are used, along with 4 protons, to reduce ... Carbon Monoxide Specifically Inhibits CytochromeC Oxidase of Human Mitochondrial Respiratory Chain ... d782 4229 97ec bb01d98a6ae0 40sessionmgr15 ref all bind to cytochromec oxidase, thus competitive ... altering cytochromec oxidase COX functionality or structure can result in severe, often fatal ... of Cytochromec Oxidase Assembly journal Physiol. Res. volume 53 Suppl. 1 pages S213 S223 url http www.biomed.cas.cz ... gallery Image Etc2.svg ETC Image Komplex IV.png Complex IV gallery See also Cytochromec oxidase subunit I Cytochromec oxidase subunit II Cytochromec oxidase subunit III References references External ... http www2.ufp.pt pedros anim 2frame iven.htm Interactive Molecular model of cytochromec oxidase ... more details
Cytochromec 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 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 purifies as a consequence of crystallization, making cycles of crystallization an effective final purification step. Much like catalase , the reaction of cytochromec peroxidase proceeds through a three step ... kraut projects.html Cytochromec peroxidase , maintained by the http chem faculty.ucsd.edu ... cytochromec peroxidase. Peroxidases DEFAULTSORT CytochromeC Peroxidase Category EC 1.11.1 Category Hemoproteins it Citocromo c perossidasi ja c ... 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
Pfam box Symbol Cytochrom C Name Cytochromec image PDB 1cry EBI.jpg width caption Structure of cytochrome c2 from Rhodopseudomonas viridis. 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 PF00034 InterPro IPR003088 SMART PROSITE PDOC00169 SCOP 1cry TCDB OPM family 78 OPM protein 1hrc PDB PDB3 1ql3 D 80 176 PDB3 1ql4 D 80 176 PDB3 1i6e A 80 176 PDB3 1c7m A 80 176 PDB3 1i6d A 80 176 PDB3 1ccr 12 111 PDB3 2b4z A 4 103 PDB3 2pcb B 4 103 PDB3 1giw 4 103 PDB3 1m60 A 4 103 PDB3 1fi7 A 4 103 PDB3 1ocd 4 103 PDB3 1lc1 A 4 103 PDB3 1lc2 A 4 103 PDB3 1crc B 4 103 PDB3 1fi9 A 4 103 ... 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 ... have several extra loops by comparison with class IB cytC. Subfamilies Bacterial cytochromec, class IC InterPro IPR008169 Human proteins containing this domain Cytochromec CYCS References reflist ... 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 ... 1c75 A 22 92 PDB3 1b7v A 22 92 PDB3 1n9c A 22 92 PDB3 1k3h A 22 92 PDB3 1k3g A 22 92 Cytochromes c cytC are electron transfer proteins having one or several heme c groups, bound to the protein by one ... haem iron ligand is always provided by a histidine residue. Cytochromes c possess a wide range of properties ... residue about 40 residues further on towards the C terminus. On the basis of sequence similarity ... more details
enzyme Name cytochromec lysine N methyltransferase EC number 2.1.1.59 CAS number 82047 78 7 IUBMB EC number 2 1 1 59 GO code 0000277 image width caption Wikify date July 2009 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. Chem. volume 253 pages 1427&ndash 35 pmid 203592 issue 5 cite journal author Nochumson S, Durban E, Kim S, Paik WK year 1977 title Cytochromec specific protein methylase III ... cite journal author Valentine J, Pettigrew GW year 1982 title A cytochromec methyltransferase ... 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 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 Wikify date July 2009 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
Pfam box Symbol COX3 Name Cytochromec oxidase subunit III image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromec oxidase. ref name pmid15299438 cite journal author Miki ... OPM family 4 OPM protein 1v55 PDB PDB3 2phv I 12 17 PDB3 1v55 C 6 261 PDB3 1occ P 6 261 PDB3 1oco C 6 261 PDB3 1ocz C 6 261 PDB3 1ocr P 6 261 PDB3 2occ C 6 261 PDB3 1v54 C 6 261 PDB3 1llk A 6 261 PDB3 1m56 I 7 266 PDB3 1m57 I 7 266 PDB3 1qle C 7 273 PDB3 1fft H 1 203 Cytochromec oxidase subunit III is one of main transmembrane subunits of cytochromec oxidase Cytochromec oxidase EC number 1.9.3.1 ... the transfer of electrons from reduced cytochromec 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 ... membrane ref name PUB00006599 cite journal author Michel H title Cytochromec oxidase catalytic cycle ... nature04619 ref . Cytochromec oxidase is an oligomeric enzymatic complex that is located in the mitochondrial ... structure of prokaryotic and eukaryotic cytochromec oxidase contains three common subunits, Cytochromec oxidase subunit I I , Cytochromec oxidase subunit II II and III . In prokaryotes, subunits I ..., rather than the single cytochromec oxidase present in the eukaryotic mitochondrial systems. Although the cytochrome o oxidases do not catalyze the cytochromec but the quinol ubiquinol oxidation they belong to the same haem copper oxidase superfamily as cytochromec oxidases. Members of this family share sequence similarities in all three core subunits Cytochromec oxidase subunit I subunit I is the most conserved subunit, whereas Cytochromec oxidase subunit II subunit II is the least conserved ... reading The whole structure of the 13 subunit oxidized cytochromec oxidase at 2.8 A. Tsukihara ... structure analysis of cytochrome c2 from Rhodopseudomonas viridis journal Acta Crystallogr. D Biol ... M, Belevich I, Verkhovsky MI title Proton coupled electron transfer drives the proton pump of cytochrome ... more details
Orphan date February 2009 Pfam box Symbol COX5B Name Cytochromec oxidase subunit Vb image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromec oxidase. ref name pmid15299438 cite journal author Miki K, Sogabe S, Uno A, et al. title Application of an automatic molecular replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis journal Acta Crystallogr. D Biol. Crystallogr. volume 50 issue Pt 3 pages 271 5 year 1994 month May pmid 15299438 doi 10.1107 S0907444993013952 url ref Pfam PF01215 InterPro IPR002124 SMART PROSITE PDOC00663 SCOP 1occ TCDB OPM family 4 OPM protein 1v55 PDB PDB3 1v55 S 30 98 PDB3 1occ S 30 98 PDB3 1v54 F 30 98 PDB3 1oco F 30 98 PDB3 1ocz S 30 98 PDB3 1ocr F 30 98 PDB3 2occ S 30 98 Cytochromec oxidase, subunit Vb is a subunit of mitochondrial cytochromec oxidase complex. Cytochromec oxidase EC number 1.9.3.1 is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochromec to oxygen ref name PUB00000581 cite journal author Capaldi RA, Malatesta F, Darley Usmar VM title Structure of cytochromec oxidase journal Biochim. Biophys. Acta volume 726 issue 2 pages 135 148 year 1983 pmid 6307356 ref . In eukaryotes this enzyme complex is located in the mitochondrial inner membrane in aerobic prokaryotes it is found in the plasma membrane. In eukaryotes, in addition to the three large subunits, I, II and III, that form ... of the 13 subunit oxidized cytochromec oxidase at 2.8 A journal Science volume 272 issue 5265 ... are clustered in the C terminal section of the subunit. Human proteins containing this domain COX5B References reflist External links http www.expasy.org cgi bin nicedoc.pl?PDOC00663 Cytochromec ... R, Sandona D, Brini M, Capaldi RA, Bisson R title The most conserved nuclear encoded polypeptide of cytochromec oxidase is the putative zinc binding subunit primary structure of subunit V from the slime ... more details
Pfam box Symbol COX1 Name CytochromeC and Quinol oxidase polypeptide I image PDB 1occ EBI.jpg width caption Structure of the 13 subunit oxidized cytochromec oxidase. ref name pmid8638158 cite journal author Tsukihara T, Aoyama H, Yamashita E, et al. title The whole structure of the 13 subunit oxidized cytochromec oxidase at 2.8 A journal Science volume 272 issue 5265 pages 1136 44 year 1996 month May pmid 8638158 doi 10.1126 science.272.5265.1136 url ref Pfam PF00115 InterPro IPR000883 SMART PROSITE PDOC00074 SCOP 1occ TCDB 3.D.4 OPM family 4 OPM protein 1v55 PDB PDB3 2occ N 5 461 PDB3 1ocr N 5 461 PDB3 1v54 A 5 461 PDB3 1occ A 5 461 PDB3 1v55 A 5 461 PDB3 1oco N 5 461 PDB3 1ocz N 5 461 PDB3 1m57 G 19 504 PDB3 1m56 A 19 504 PDB3 1qle A 21 496 PDB3 1ehk A 218 309 PDB3 1fft A 47 505 PDB3 1xme A 18 108 CytochromeC and Quinol oxidase polypeptide I is main subunit of cytochromec oxidase complex. Cytochromec oxidase EC number 1.9.3.1 is a key enzyme in aerobic metabolism. Proton pumping heme copper oxidases represent the terminal, energy transfer enzymes of respiratory chains in prokaryotes ... I of cytochromec and ubiquinol oxidases EC number 1.10.3 , is directly involved in the coupling ... Usmar VM title Structure of cytochromec oxidase journal Biochim. Biophys. Acta volume 726 issue 2 ... from cytochromec oxidase in Gram positive bacteria and that archaebacterial quinol oxidase has ... and eubacteria and is a heterodimer of cytochromes b and c. Phenazine methosulphate can act as acceptor. Subfamilies Cytochromec oxidase cbb3 type, subunit I InterPro IPR004677 Cytochrome o ubiquinol oxidase, subunit I InterPro IPR014207 Cytochrome aa3 quinol oxidase, subunit I InterPro IPR014233 Cytochromec oxidase, subunit I bacterial type InterPro IPR014241 Human proteins containing this domain ... J, Higgins DG, Lubben M title Evolution of cytochrome oxidase, an enzyme older than atmospheric ..., Wikstrom M title Structural models of the redox centres in cytochrome oxidase journal EMBO J. volume ... more details
enzyme Name ubiquinol cytochromec reductase EC number 1.10.2.2 CAS number 9027 03 6 IUBMB EC number ... cytochromec , whereas its 3 product chemistry products are quinone Q , ferro Fe sup 2 sup cytochrome ... schematic illustration of complex III reactions The coenzyme Q cytochromec oxidoreductase , sometimes ... . 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 ... c1 oxidoreductase, CoQH2 cytochromec oxidoreductase, ubihydroquinol cytochromec oxidoreductase, coenzyme QH2 cytochromec reductase, and QH2 cytochromec oxidoreductase. Structure Image Cytochrome ... b subunit has two b type heme s b sub L sub and b sub H sub , the cytochromec subunit has one c type heme Cytochrome C1 c sub 1 sub , and the Rieske Iron Sulfur Protein subunit ISP has a two iron, two ... the reduction of Cytochromeccytochromec by oxidation of coenzyme Q CoQ and the concomitant ... c Fe sup III sup 2 H sup sup sub in sub Q 2 cytochromec Fe sup II sup 4 H sup sup sub out sub ... IM and two electrons are passed to cytochromec . Reaction Mechanism Image Theqcycle.gif thumb 400px The Q cycle The reaction mechanism for complex III Cytochrome bc1 , Coenzyme Q CytochromeC Oxidoreductase ... c not to be confused with cytochrome c1 , and the BH Heme transfers its electron to a nearby ubiquinone, resulting in the formation of a ubisemiquinone. Cytochromec diffuses and the fully oxidized ... the BL heme to the BH Heme. Cytocrome c1 then transfers its electron cytochromec , whilst the nearby ... EC year 1977 title Polypeptide composition of purified QH2 cytochromec oxidoreductase from beef ... more details
Pfam box Symbol COX2 TM Name Cytochromec oxidase subunit II, transmembrane domain image 1qle opm.gif width 250 caption Bacterial cytochromec oxidase complex. Subunit II indicated by blue. Pfam PF02790 InterPro IPR011759 SMART PROSITE PDOC00075 SCOP 1occ TCDB 3.D.4 OPM family 4 OPM protein 1v55 PDB PDB3 1v54 B 2 83 PDB3 1ocz B 1 83 PDB3 2occ B 1 83 PDB3 1ocr B 1 83 PDB3 1oco B 1 83 PDB3 1v55 B 2 83 PDB3 1occ O 1 83 PDB3 1m57 B 35 122 PDB3 1m56 H 35 122 PDB3 1qle B 41 128 Pfam box Symbol COX2 Name CytochromeC oxidase subunit II, periplasmic domain image width caption Pfam PF00116 InterPro IPR002429 SMART PROSITE PDOC00075 SCOP 1occ TCDB 3.D.4 OPM family 4 OPM protein 1v55 PDB PDB3 1v54 B 95 214 PDB3 1ocz B 95 214 PDB3 2occ B 95 214 PDB3 1ocr B 95 214 PDB3 1oco B 95 214 PDB3 1v55 B 95 214 PDB3 ... 1cyw 129 225 PDB3 1cyx 129 225 PDB3 1fwx C 572 648 PDB3 1qni B 489 579 PDB3 1ehk B 92 167 PDB3 2cua A 59 134 PDB3 1xme B 59 134 Cytochromec oxidase subunit II , abbreviated CoxII , is the second subunit of cytochromec oxidase . Cytochromec oxidase EC number 1.9.3.1 ref name PUB00000581 cite journal author Capaldi RA, Malatesta F, Darley Usmar VM title Structure of cytochromec oxidase journal ... chain and is involved in the transfer of electrons from cytochromec to oxygen. In eukaryotes ... Cu A see InterPro IPR001505 , probably the primary acceptor in cytochromec oxidase. An exception is the corresponding ... CO II have a C terminal extension that contains a covalently bound haem c. The N terminal domain of cytochromeC oxidase contains two transmembrane alpha helices. Human proteins containing this domain ... oxidized cytochromec oxidase at 2.8 A. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H ... polypeptides mammals . In Leigh s disease , there may be an abnormality or deficiency of cytochrome oxidase. Subunit 2 CO II transfers the electrons from cytochromec to the Main subunit of cytochromec oxidase catalytic subunit 1 . It contains two adjacent transmembrane regions in its N terminus and the major ... more details
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 c subunit H sub 2 sub O math rightleftharpoons math trimethylamine N oxide 2 ferrocytochrome c subunit 2 H sup sup The 3 substrate biochemistry substrates of this enzyme are trimethylamine , ferricytochrome c subunit , and water H sub 2 sub O , whereas its 3 product chemistry products are trimethylamine N oxide , ferrocytochrome c subunit , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is trimethylamine cytochromec oxidoreductase . Other names in common use include TMAO reductase , and TOR . This enzyme participates in two component system general . References reflist 1 cite journal author Arata H, Shimizu M, Takamiya K date Tokyo title Purification and properties of trimethylamine N oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans journal J. volume Biochem. pages 470&ndash 5 pmid 1337081 issue 4 cite journal doi 10.1515 bchm.1997.378.3 4.293 author Knablein J, Dobbek H, Ehlert S, Schneider F date 1997 title Isolation, cloning, sequence analysis and X ray structure of dimethyl sulfoxide trimethylamine N oxide reductase from Rhodobacter capsulatus 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
Image Cytochrome c.png thumb 250px Cytochromec with heme c . Cytochromes are, in general, membrane bound ... as Protein subunit monomeric protein s e.g., cytochromec or as Protein subunit subunits of bigger ... pyridine ligated state, i.e., 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 ... potential. Three 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 ... a and a sub 3 sub Cytochromec oxidase Complex IV with electrons delivered to complex by soluble cytochromec hence the name b and Cytochrome C1 c sub 1 sub Coenzyme Q cytochromec reductase Complex III b sub 6 sub and Cytochrome f f Plastoquinol plastocyanin reductase A completely distinct family of cytochromes is known as the cytochrome P450 oxidase s, so named for the characteristic Soret ... doi 10.1098 rstl.1886.0007 url http www.jstor.org pss 109482 pages 267 298 author1 Mac Munn, C ... band in the reduced state, as cytochromes a 605 nm , b 565 nm , and c 550 nm . The UV ... across the membrane, and assembly of flagellum flagella . Types Several kinds of cytochrome exist and can ... Category Cytochromes cs Cytochrom de Cytochrome es Citocromo eo Citokromo eu Zitokromo fr Cytochrome id Sitokrom it Citocromi he mk ja pl Cytochromy pt Citocromo ru ... more details
Move to Commons Summary By Richard Wheeler User Zephyris Zephyris 2006. 17 NMR structures of cytochromec illustrating the dynamics of a protein in solution. Made with pymol and PDB 2NEW . Licensing GFDL self with disclaimers migration relicense ... more details
Cytochrome C1 is formed in the cytosol and protein targeting targeted to the mitochondrial intermembrane space. It is one of the constituents of Coenzyme Q cytochromec reductase complex III , which forms the third proton pump in the mitochondrial electron transport chain . Cytochromec sub 1 sub is a subunit of the electron transport chain protein ubiquinol cytochromec reductase Ubiquinol Cytochromec Reductase UQCR, Complex III or Cytochrome bc1 complex , which consists of the products of one mitochondrially encoded gene, MT CYB MTCYTB mitochondrial cytochrome b and ten nuclear genes UQCRC1 , UQCRC2 , Cytochrome c1, UQCRFS1 Rieske protein , UQCRB , UQCRQ http www.ncbi.nlm.nih.gov nuccore 98986462 11kDa protein , UQCRH cyt c1 Hinge protein , Rieske Protein presequence, cyt. c1 associated protein , and UQCR http www.ncbi.nlm.nih.gov nucleotide 19923785 Rieske associated protein . External links MeshName Cytochrome c1 Category Peripheral membrane proteins membrane protein stub ... more details
morefootnotes date September 2010 Cytochrome f is the largest subunit of cytochrome b6f complex cytochrome b sub 6 sub f complex plastoquinol&mdash plastocyanin reductase EC number 1.10.99.1 . The crystal structures of soluble lumen side domain of cytochrome f reveal two structural domains a small one above a larger one, which, in turn, is on top of the attachment to the membrane domain. The large domain consists of an antiparallel sandwich and a short heme binding peptide , which form a three layer structure. The small domain is inserted between two strands of the large domain and is an all domain. The heme is bound between two short helices at the N terminus of cytochrome f . Within the second helix is the sequence motif for the c type cytochromes, Cys Xaa Xaa Cys His, which is covalently attached to the heme through thioether bonds of the two cysteine Residue chemistry residue s. The fifth heme iron ligand is histidine and the sixth heme iron ligand is the amino group of N terminal tyrosine residue Tyr 1 . Cytochrome f has an internal network of water molecules. It has been hypothesized that this water chain functions as a proton wire. The water chain appears to be a conserved ... of cytochrome f journal Photosynth. Res. year 2004 volume 80 pages 265 276 pmid 16328825 doi 10.1023 ... aspects of the cytochrome b sub 6 sub f complex structure of the lumen side domain of cytochrome f ... The heme redox center of chloroplast cytochrome f is linked to a buried five water chain journal ... cite journal author Prince, R.C. and George, G.N. title Cytochrome f revealed journal Trends ... issue 6 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 Category Photosynthesis ... more details
cytochrome bc1 complex Pfam PF00033 InterPro IPR005797 SMART PROSITE PDOC00171 SCOP 3bcc TCDB 3.D.3 OPM family 3 OPM protein 1bcc PDB PDB3 1bcc C 10 205 PDB3 2e74 A 10 205 PDB3 1l0l C 9 204 PDB3 1ntk C 9 204 PDB3 1ntm C 9 204 PDB3 1ntz C 9 204 PDB3 1sqq C 9 204 PDB3 1l0n C 9 204 PDB3 1sqx C 9 204 PDB3 1nu1 C 9 204 PDB3 1sqv C 9 204 PDB3 1sqb C 9 204 PDB3 1be3 C 9 204 PDB3 1sqp C 9 204 PDB3 1kb9 C 8 205 PDB3 1p84 C 8 205 PDB3 1kyo C 8 205 PDB3 1q90 B 9 210 PDB3 1vf5 A 9 210 PDB3 2d2c N 9 210 Cytochrome b b6 is the main subunit of transmembrane cytochrome bc1 complex cytochrome bc1 and Cytochrome ... conservation of protein regions in the protonmotive cytochrome b and their possible roles in redox ... S, Crimi M, Ghelli A, Patarnello T, Meyer A title Mitochondrial cytochrome b evolution and structure ... and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III EC number 1.10.2.2 also known as the bc1 complex or ubiquinol cytochromec reductase. In plant chloroplasts and cyanobacteria, there is an analogous protein, cytochrome b6, a component of the plastoquinone ... role in the cell. Structure 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 ... T, Meyer A, De Vries S title Mitochondrial cytochrome b evolution and structure of the protein ... that probably has 8 transmembrane 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 ... atoms of these two heme groups. Use in phylogenetics Cytochrome b is commonly used to determine ... studies involving cytochrome b have resulted in new classification schemes and have been ... relationships. ref name 2001Castresana cite journal last1 Castresana first1 J. title Cytochrome b ... 4 ref Clinical significance Mutations in cytochrome b primarily result in exercise intolerance in human ... more details
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 ... are water soluble. The family of cytochrome b sub 5 sub like proteins includes besides cytochrome b ... cytochrome b sub 2 sub small L small lactate dehydrogenase EC number 1.1.2.3 , sulfite oxidase EC ... 1.7.1.3 , and plant and fungal cytochrome b sub 5 sub acyl lipid desaturase fusion proteins. Structure 3 D structures of a number of cytochrome b sub 5 sub and yeast flavocytochrome b sub 2 sub are known ... by spatially close N terminal and C terminal segments. The two histidine residues provide the fifth ... crevice. Two isomers of cytochrome b sub 5 sub , referred to as the A major and B minor forms, differ by a 180 rotation of the heme about an axis defined by the and meso carbons. Cytochrome b sub 5 sub in some biochemical reactions EC number 1.6.2.2 cytochrome b5 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 ... 6 issue 2 cite journal author Rivera, M., Barillas Mury, C., Christensen, K.A., Little, J.W., Wells ... studies of the rat outer mitochondrial membrane cytochrome b sub 5 sub journal Biochemistry year 1992 ... Schenkman, J.B. and Jansson, I. title The many roles of cytochrome b sub 5 sub journal Pharmacol ... 2 External links PDB 1B5A Solution structure of rat cytochrome b sub 5 sub form A PDB 1B5B Solution 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
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 ... of Cytochrome P450 Proteins Metal Ions in Life Sciences edition language publisher Wiley location New ... cite journal author Danielson PB title The cytochrome P450 superfamily biochemistry, evolution ... title Cytochrome P450 Homepage author Nelson D authorlink coauthors date work publisher ... Cytochrome P450 Homepage and allele names http www.cypalleles.ki.se CYP Allele Nomenclature Committee ... The active site of cytochrome P450 contains a heme iron center. The iron is tethered to the P450 protein ... SGNH x GD F RKHPT P u C u LIVMFAP GAD . ref http www.expasy.org cgi bin nicedoc.pl?PDOC00081 PROSITE ... S title Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes journal Chem. Rev. volume ... cite journal author Poulos TL, Finzel BC, Howard AJ title High resolution crystal structure of cytochrome .... Paul R. Ortiz de Montellano authorlink editor others title Cytochrome P450 structure, mechanism, and biochemistry ... state of the active site favors the transfer of an electron from NAD P H via cytochrome P450 reductase ... GG, Schenkman JB title Spin state control of the hepatic cytochrome P450 redox potential journal ... 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 group. This is a short ... is shown in the diagram. C If carbon monoxide CO binds to reduced P450, the catalytic cycle is interrupted ... 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 . FR Fd P450 ... both electrons required by the CYP come from cytochrome b5 . FMN Fd P450 systems originally found ... 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
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
, Millett F title Effect of modification of individual cytochromec lysines on the reaction with cytochrome ...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 ... reticulum . It has a C terminal transmembrane alpha helix. Isoform 2 was found in cytoplasm ... 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 ... more details
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