of the cytochromeb6fcomplex quinone analogue inhibitors as ligands of heme cn. journal J Mol Biol ... Cytochromeb6fComplex from Nostoc sp. PCC 7120. journal J Biol Chem volume 284 ... of photosynthesis time independent structure of the cytochromeb6fcomplex. journal Biochemistry volume .... last3 Smith first3 JL. last4 Cramer first4 WA. title Structure of the cytochromeb6fcomplex of oxygenic ... AND OLD CONTROVERSIES CONCERNING THE CYTOCHROMEb6fCOMPLEX OF OXYGENIC PHOTOSYNTHESIS. journal ... and related complexes in membranes MeshName Cytochromeb6fComplex Multienzyme complexes Proton ...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 cytochromeb6fcomplex 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 complexcytochrome 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 ... first4 D. title An atypical haem in the cytochrome b 6 f complex. journal Nature volume 426 issue 6965 ... between cytochrome b of mitochondrial complex III and the chloroplast b6 f complex position of the cytochrome ... b6fcomplex. journal Photochem Photobiol volume 84 issue 6 pages 1349 58 month year doi 10.1111 j.1751 ... function In photosynthesis , the cytochrome b sub 6 sub f complex functions to mediate the transfer ... ATP in chloroplasts. ref name Voet In a separate reaction, the cytochrome b sub 6 sub f complex ... b6fcomplex. journal Annu Rev Biochem volume 75 issue pages 769 90 month year 2006 doi ... transfer In contrast to Complex III, cytochrome b sub 6 sub f catalyzes another electron transfer reaction ... more details
and related metabolic pathways class wikitable Cytochromes Combination a and a sub 3 sub Cytochrome c oxidase Complex IV with electrons delivered to complex by soluble cytochrome c hence the name b and Cytochrome C1 c sub 1 sub Coenzyme Q cytochrome c reductase Complex III b sub 6 sub and Cytochrome ...Image Cytochrome c.png thumb 250px Cytochrome c with heme c . Cytochromes are, in general, membrane bound hemoprotein s that contain heme groups and carry out electron transport . They are found either as Protein subunit monomeric protein s e.g., cytochrome c or as Protein subunit subunits of bigger enzymatic complexes that catalyze redox reactions. History Cytochromes were initially described in 1884 by MacMunn as respiratory pigments myohematin or histohematin . ref name MacMunn cite journal doi 10.1098 rstl.1886.0007 jstor 109482 pages 267 298 author1 Mac Munn, C. A issue 0 title Researches on Myohaematin and the Histohaematins journal Philosophical Transactions of the Royal Society of London ..., the pyridine hemochrome method. Within each class, cytochrome a , b , or c , early cytochromes are numbered ... membrane bound and soluble complex chemistry complex es and cofactor biochemistry cofactor s are involved ... 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 ... 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 complexcytochrome bc1 complex bears extensive analogy to the cytochromeCytochromeb6fcomplexb6fcomplex 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
, 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 ... 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 ... more details
cytochrome bc1 complex Pfam PF00033 InterPro IPR005797 SMART PROSITE PDOC00171 SCOP 3bcc ..., 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 number 1.10.99.1 , also known as the b6fcomplex. These complexes are involved in electron transport ... 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 complexcytochrome bc1 and Cytochromeb6fcomplexb6f complexes. ref name pmid2509716 cite journal author Howell N title Evolutionary conservation 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 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 ... 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 Cytochromecomplex , 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 ... to hold the complex proteins that have other prosthetic groups as well as heme c. Applications Cytochrome ... of cytochrome c with cytochrome bc1 complex of the mitochondrial respiratory chain journal Biochim ... 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 1 Apaf 1 . ref name entrez Cytochrome c can catalyze several ... 4 thiomethyl butyric acid and 4 aminoantipyrine. Species distribution Cytochrome c is a highly conserved ... ensiweb 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 ... books?id zdeWdF NQhEC&pg PA79&lpg PA79&dq chimpanzee rhesus cytochrome c&source web&ots .... ref 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 ... 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 ... , PDB2 2axt Cytochrome b559 is an important component of Photosystem II . PSII is a multisubunit protein pigment complex containing polypeptides both intrinsic and extrinsic to the photosynthetic membrane ... of the complex, the chlorophyll and beta carotene pigments are mainly bound to the antenna proteins ... conversion process. The PSII oxygen evolving complex OEC provides electrons to re reduce the PSII ... 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 ... equivalents are available, this complex may remain stable, allowing the degree of binding to be determined ..., 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 ... i.e., 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 ... 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
transport chain. Complex IV is at the right. The enzyme cytochrome c oxidase or Complex IV PDB 2OCC , EC number 1.9.3.1 is a large transmembrane protein complex found in bacteria and the mitochondrion ..., 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 ...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 ... located in the mitochondrial or bacterial membrane. It receives an electron from each of four cytochrome ... triphosphate ATP . Structure Image Cmplx4.PNG thumb 300px Subunit I and II of Complex IV excluding all other subunits, PDB 2EIK The complex is a large integral membrane protein composed of several ... 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 ... Site of assembly is believed to occur near Mitochondrial membrane transport protein TOM TIM, where complex ... more details
The Complex may refer to The Complex An Insider Exposes the Covert World of the Church of Scientology , 2008 book by John Duignan The Complex How the Military Invades Our Everyday Lives , 2008 book by Nick Turse The Complex album The Complex album , by Blue Man Group The Complex Valdosta, Georgia , a multi purpose arena See also Complex disambiguation disambig ... more details
wiktionary complex complexes A complex is a whole that comprehends a number of intricate parts, especially one with interconnected or mutually related parts for example, a complex of building s . Complex may refer to tocright Biology Multiprotein complex , a group of two or more associated polypeptide chains Complex taxonomy , in biology, a cluster of species so closely related that they intergrade ... complex , a complex system of organisms and dependencies involved in a case of mimicry Chemistry Coordination complex , also called a coordination compound or metal complex , a structure consisting ... complex , a coordination complex with more than one bond Mathematics Complex number , an extension of real numbers obtained by adjoining imaginary numbers Complex system , a system of interconnected simple ... order behavior Complex analysis , the study of functions of complex numbers An element of a complex algebra or field of sets Chain complex , a possibly long sequence of maps Simplicial complex , a kind ... CW complex , or closure finite weak complex, a kind of topological space, a generalization of the simplicial complex Line complex , a 3 dimensional family of lines in space Other scientific uses Complex psychology , a group of mental factors that are unconsciously associated by the individual with a particular subject and influence the individual s attitude and behavior Synonym for a complex system which generally includes all interactions between elements Complex crater , a type of large impact crater morphology As a name Complex artist , an American Rap artist Complex band , a Japanese rock band Complex magazine Complex magazine , a young men s style lifestyle magazine CoMPLEX ucl is an interdisciplinary centre at University College London into biology and biomedicine Complex song Complex song , a song by British musician Gary Numan See also The Complex disambiguation Complexity Complexity disambiguation Complexity theory disambiguation Theory of complex systems The Military ... 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
PBB geneid 1535 Cytochrome b 245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis. ref name pmid2243141 cite journal author Dinauer MC, Pierce EA, Bruns GA, Curnutte JT, Orkin SH title Human neutrophil cytochrome b light chain p22 phox . Gene structure, chromosomal location, and mutations in cytochrome negative autosomal recessive chronic granulomatous disease journal J Clin Invest volume 86 issue 5 pages 1729 37 year 1990 month Dec pmid 2243141 pmc 296926 doi 10.1172 JCI114898 ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Cytochrome b is composed of a light chain alpha and a heavy chain beta . This gene encodes the light, alpha subunit, which has been proposed as a primary component of the microbicidal oxidase ... Gene CYBA cytochrome b 245, alpha polypeptide url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ... cite journal author de Boer M, de Klein A, Hossle JP, et al. title Cytochrome b558 negative, autosomal recessive chronic granulomatous disease two new mutations in the cytochrome b558 light chain of the NADPH ... mutation in the cytoplasmic domain of the neutrophil p22 phox cytochrome b subunit is associated ... cite journal author Bu Ghanim HN, Casimir CM, Povey S, Segal AW title The alpha subunit of cytochrome ... al. title Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils ... CA, Allen RA, Cochrane CG, Jesaitis AJ title Purified cytochrome b from human granulocyte plasma ... expression of the 22 kilodalton light chain of human neutrophil cytochrome b. journal Proc. Natl ... chain of cytochrome b558 of the human NADPH oxidase p22 phox leads to defective translocation ... in the assembly of the NADPH oxidase complex by peptide walking . journal J. Biol. Chem ... AM title Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial ... more details
Pfam box Symbol Cytochrom C Name Cytochrome c 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 PDB3 1hrc 4 103 PDB3 1i5t A 4 103 PDB3 1u75 B 4 103 PDB3 1akk 4 103 PDB3 1wej F 4 103 PDB3 2frc 4 103 PDB3 2giw 4 103 PDB3 1j3s A 4 103 PDB3 1i55 A 3 102 PDB3 1lfm A 3 102 PDB3 1i54 B 3 102 PDB3 3cyt ... family Symbol Cytochrom C 2 Name Cytochrome C image PDB 1bbh EBI.jpg width caption atomic structure of a cytochrome c with an unusual ligand controlled dimer dissociation at 1.8 angstroms resolution ... OPM protein CAZy CDD Infobox protein family Symbol Cytochrom CIII Name Class III cytochrome C family ... of the 16 heme cytochrome c 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 cytochrome c mitochondrial cytochrome ... of a cytochrome c with an unusual ligand controlled dimer dissociation at 1.8 A resolution journal ... ref Class IV includes complex proteins containing other prosthetic groups besides haem c, such as flavocytochromes c and cytochromes cd. ref name PUB00000610 Subfamilies Bacterial cytochrome c, class IC InterPro IPR008169 Human proteins containing this domain Cytochrome c CYCS References reflist InterPro ... 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 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
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