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cytochrome c peroxidase wikipedia jump to content main menu main menu move to sidebar hide navigation main page contents current events random article about wikipedia contact us contribute help learn to edit community portal recent changes upload file special pages search search appearance donate create account log in personal tools donate create account log in contents move to sidebar hide top 1 amino acid composition 2 references 3 external links toggle the table of contents cytochrome c peroxidase 7 languages العربية español français italiano 日本語 srpskohrvatski српскохрватски српски srpski edit links article talk english read edit view history tools tools move to sidebar hide actions read edit view history general what links here related changes upload file permanent link page information cite this page get shortened url switch to legacy parser print export download as pdf printable version in other projects wikimedia commons wikidata item appearance move to sidebar hide from wikipedia the free encyclopedia cytochrome c peroxidase identifiers ec no 1 11 1 5 cas no 9029 53 2 databases brenda enzyme data expasy nicezyme view kegg enzyme entry metacyc metabolic pathway rhea reactions pdb structures rcsb pdb pdbe pdbsum gene ontology amigo quickgo search pmc articles pubmed articles ncbi proteins cytochrome c peroxidase identifiers organism saccharomyces cerevisiae symbol ccp orthologs oma entry uniprot p00431 search for structures swiss model domains interpro cytochrome c peroxidase ccp or ccp 1 is a water soluble heme containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c and reduces hydrogen peroxide to water ccp h 2 o 2 2 ferrocytochrome c 2h ccp 2h 2 o 2 ferricytochrome c ccp can be derived from aerobically grown yeast strains and can be isolated in both native and recombinant forms with high yield from saccharomyces cerevisiae the enzyme s primary function is to eliminate toxic radical molecules produced by the cell which are harmful to biological systems it works to maintain low concentration levels of hydrogen peroxide which is generated by the organism naturally through incomplete oxygen reduction when glucose levels in fast growing yeast strains are exhausted the cells turn to respiration which raises the concentration of mitochondrial h 2 o 2 2 in addition to its peroxidase activity it acts as a sensor and a signaling molecule to exogenous h 2 o 2 which activates mitochondrial catalase activity 3 in eukaryotes ccp contain a mono b type haem cofactor and is targeted to the intermembrane space of the mitochondria in prokaryotes ccp contains a c type diheme cofactor and is localized to the periplasm of the cell both enzymes work to resist peroxide induced cellular stress 4 ccp plays an integral role in enabling inter protein biological electron transfer the negative charge transfer process is carried out by a complex formed between cytochrome c and cytochrome c peroxidase which occurs in the inter membrane space of mitochondria the mechanism involves ferrous cytochrome c cc providing electrons for the cc ccp system to reduce hydrogen peroxide to water 5 the complex is formed by non covalent interactions 6 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 7 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 structure was the work of thomas poulos and coworkers in the late 1970s 8 ccp is the first heme enzyme to have its structure successfully solved through x ray crystallography the yeast enzyme is a monomer of molecular weight 34 000 containing 293 amino acids and contains as well a single non covalently bound heme b it is negatively charged and is a moderately sized enzyme 34 2 kda the apoenzyme not active and bound to substrates has an acidic isoelectric point of ph 5 0 5 2 9 unusual for proteins this enzyme crystallizes when dialysed against distilled water more so the enzyme purifies as a consequence of crystallization making cycles of crystallization an effective final purification step much like catalase the reaction of cytochrome c peroxidase proceeds through a three step process forming first a compound i and then a compound ii intermediate ccp rooh compound i roh h 2 o ccp compound i e h compound ii compound ii e h ccp ccp catalyzed redox cycle ccp in the resting state has a ferric heme and after the addition of two oxidizing equivalents from a hydroperoxide usually hydrogen peroxide it becomes oxidized to a formal oxidation state of 5 fe v commonly referred to as ferryl heme however both low temperature magnetic susceptibility measurements and mössbauer spectroscopy show that the iron in compound i of ccp is a 4 ferryl iron with the second oxidizing equivalent existing as a long lived free radical on the side chain of the tryptophan residue trp 191 10 in its resting state the fe atom fe iii in the ccp heme is paramagnetic with high spin s 5 2 once the catalytic cycle is initiated the iron atom is oxidized to form an oxyferryl intermediate fe iv o which has low spin s 1 2 5 this is different from most peroxidases which have the second oxidizing equivalent on the porphyrin instead compound i of ccp is fairly long lived decaying to ccp compound ii with a half life at room temperature of 40 minutes to a couple hours ccp has high sequence identity to the closely related ascorbate peroxidase enzyme amino acid composition edit ccp shows an unusual amino acid pattern compared to other peroxidase plant peroxidase such as horseradish peroxidase and pineapple peroxidase b have low lysine tryptophan and tyrosine contents and high cysteine content in contrast ccp has high lysine tryptophan and tyrosine content and low cysteine content 11 the enzyme contains a 68 residue sequence at the n terminus of its monomeric protein which targets it to the inter membrane space of the mitochondria where it can the complex with cytochrome c and where it carries out its sensor signaling and catalytic roles 2 studies indicate the distal arginine arg48 a highly conserved amino acid among peroxidase plays an important role in the catalytic activity of ccp by controlling its active site through stabilization of the reactive oxyferryl intermediate from control of its access 12 references edit fischer marcus coleman ryan g fraser james s shoichet brian k july 2014 incorporation of protein flexibility and conformational energy penalties in docking screens to improve ligand discovery nature chemistry 6 7 575 583 doi 10 1038 nchem 1954 issn 1755 4330 pmc 4144196 pmid 24950326 1 2 kathiresan m martins d english am december 2014 respiration triggers heme transfer from cytochrome c peroxidase to catalase in yeast mitochondria proceedings of the national academy of sciences of the united states of america 111 49 17468 73 bibcode 2014pnas 11117468k doi 10 1073 pnas 1409692111 pmc 4267377 pmid 25422453 martins d kathiresan m english am december 2013 cytochrome c peroxidase is a mitochondrial heme based h2o2 sensor that modulates antioxidant defense free radical biology medicine 65 541 51 doi 10 1016 j freeradbiomed 2013 06 037 pmid 23831190 atack jm kelly dj 2007 structure mechanism and physiological roles of bacterial cytochrome c peroxidases advances in microbial physiology 52 73 106 doi 10 1016 s0065 2911 06 52002 8 isbn 9780120277520 pmid 17027371 cite journal cs1 maint periodical has isbn link 1 2 volkov an nicholls p worrall ja november 2011 the complex of cytochrome c and cytochrome c peroxidase the end of the road biochimica et biophysica acta bba bioenergetics 1807 11 1482 503 doi 10 1016 j bbabio 2011 07 010 pmid 21820401 guo m bhaskar b li h barrows tp poulos tl april 2004 crystal structure and characterization of a cytochrome c peroxidase cytochrome c site specific cross link proceedings of the national academy of sciences of the united states of america 101 16 5940 5 bibcode 2004pnas 101 5940g doi 10 1073 pnas 0306708101 pmc 395902 pmid 15071191 altchul am abrams r hogness tr 1941 cytochrome c peroxidase pdf j biol chem 136 3 777 794 doi 10 1016 s0021 9258 18 73036 6 poulos tl freer st alden ra edwards sl skogland u takio k eriksson b xuong n yonetani t kraut j january 1980 the crystal structure of cytochrome c peroxidase pdf the journal of biological chemistry 255 2 575 80 doi 10 1016 s0021 9258 19 86214 2 pmid 6243281 yonetani t 1970 cytochromec peroxidase cytochrome c peroxidase advances in enzymology and related areas of molecular biology vol 33 pp 309 35 doi 10 1002 9780470122785 ch6 isbn 9780470122785 pmid 4318313 sivaraja m goodin db smith m hoffman bm august 1989 identification by endor of trp191 as the free radical site in cytochrome c peroxidase compound es science 245 4919 738 40 bibcode 1989sci 245 738s doi 10 1126 science 2549632 pmid 2549632 ellfolk n 1967 cytochrome c peroxidase 3 the amino acid composition of cytochrome c peroxidase of baker s yeast acta chemica scandinavica 21 10 2736 42 doi 10 3891 acta chem scand 21 2736 pmid 5585683 iffland a tafelmeyer p saudan c johnsson k september 2000 directed molecular evolution of cytochrome c peroxidase biochemistry 39 35 10790 8 doi 10 1021 bi001121e pmid 10978164 external links edit cytochrome c peroxidase maintained by the kraut research group the uniprot entry for yeast cytochrome c peroxidase v t e oxidoreductases peroxidases ec 1 11 1 11 1 1 14 nadh peroxidase nadph peroxidase fatty acid peroxidase catalase cytochrome c peroxidase eosinophil peroxidase glutathione peroxidase gpx 1 2 3 4 5 6 7 8 horseradish peroxidase lactoperoxidase myeloperoxidase thyroid peroxidase deiodinase iodothyronine deiodinase iodotyrosine deiodinase 1 11 1 15 peroxiredoxin 1 2 3 4 5 6 v t e enzymes activity active site binding site catalytic triad oxyanion hole enzyme promiscuity diffusion limited enzyme cofactor enzyme catalysis regulation allosteric regulation cooperativity enzyme inhibitor enzyme activator classification ec number enzyme superfamily enzyme family list of enzymes kinetics enzyme kinetics eadie hofstee diagram hanes woolf plot lineweaver burk plot michaelis menten kinetics types ec1 oxidoreductases list ec2 transferases list ec3 hydrolases list ec4 lyases list ec5 isomerases list ec6 ligases list ec7 translocases list portal biology retrieved from https en wikipedia org w index php title cytochrome_c_peroxidase oldid 1347111247 categories ec 1 11 1 hemoproteins hidden categories protein pages needing a picture cs1 maint periodical has isbn this page was last edited on 4 april 2026 at 19 27 utc page was rendered with parsoid text is available under the creative commons attribution sharealike 4 0 license additional terms may apply by using this site you agree to 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