1.11.1.5	evolution	MacA belongs to the family of diheme cytochrome c peroxidases	-, 724337	
1.11.1.5	malfunction	an enzyme knockout mutant DELTAZmcytC exhibits filamentous shapes and reduction in growth under a shaking condition at a high temperature compared to the parental strain and became hypersensitive to exogenous H2O2. Under the same condition, the mutation causes increased expression of genes for three other antioxidant enzymes. Peroxidase activity almost abolished in mutant DELTA ZmcytC. The enzyme knockout mutant strain shows activity with ubiquinol-1 as a substrate but not with reduced horse heart cytochrome c, and it shows antimycin A-sensitive NADH oxidase activity	725756	
1.11.1.5	malfunction	significantly higher H2O2 accumulation in ccp1-null cells and catalytically inactive Ccp1W191F mutant cells. Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1	-, 725070	
1.11.1.5	malfunction	while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction	724658	
1.11.1.5	metabolism	bacterial diheme c-type cytochrome peroxidases catalyze the periplasmic reduction of hydrogen peroxide to water. CcpA does not seem to be part of a CymAMtrA-FccA-based electron transfer network in the periplasm of Shewanella oneidensis	724008	
1.11.1.5	additional information	CcP requires reductive activation for full activity. The rates of catalysis and activation differ between maltose-binding-protein-fusion and tag-free CcP and also depend on the identity of the electron donor	724366	
1.11.1.5	additional information	cytochrome c peroxidase-cytochrome c complex: the binding interface between LmP and LmCytc has one strong and one weak ionic interaction, the Lm redox pair is more dependent on ionic interactions than on nonpolar interactions	726385	
1.11.1.5	additional information	enzyme-cytochrome c protein-protein docking and modeling, overview	724335	
1.11.1.5	additional information	His175 and Asp235 in the proximal heme pocket form another H-bonding cluster that provides a proton-binding site that is responsive to changes in the redox state of the heme iron. Arg-48 is not a good candidate for the proton-binding site. Arg48 interacts with multiple waters, is located near the bottom of the solvent-access channel in CcP. The carboxylate group of heme propionate-7, His181, and Asp37 form a hydrogen-bonded cluster near the heme iron	-, 725645	
1.11.1.5	additional information	resting ferric (FeIII) Ccp1III is oxidized by H2O2 to compound I,which has a FeIV heme and a cation radical on residue W191. Compound I reacts with ferrous (FeII) Cyc1II to form compound II with a FeIV heme but no W191 radical. Reaction with a second Cyc1II reduces the FeIV heme to yield resting Ccp1III. The Ccp1W191F variant rapidly reacts with H2O2 but is very slowly reduced by Cyc1II such that it exhibits negligible Cyc1II-oxidizing activity, reaction mechanism, overview	-, 725070	
1.11.1.5	additional information	structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron	724463	
1.11.1.5	additional information	the catalytic mechanism of H2O2 reduction involves formation of CcP Compound I (CpdI), an intermediate oxidized 2 equiv above the CcP Fe(III) resting state and containing Fe(IV)=O heme oxyferryl and W191 cation radical. Subsequent CpdI reduction occurs in two one-electron steps, involving complex formation with ferrous Cc, intermolecular electron transfer (ET), and product dissociation	724372	
1.11.1.5	physiological function	bacterial di-heme cytochrome c peroxidases (CcpAs) protect the cell from reactive oxygen species by reducing hydrogen peroxide to water	705165	
1.11.1.5	physiological function	CcP catalyzes reduction of hydroperoxides using the electrons provided by its physiological binding partner cytochrome c	724372	
1.11.1.5	physiological function	CCP1 does not affect cell respiration under cyanide treatment, but predominantly detoxifies H2O2 by glutathione. CCP1 deficiency stimulates superoxide dismutase and alcohol dehydrogenase Adh1 activity and enhances catalase-peroxidase KatG, erythroascorbate peroxidase EAPX1, and glutathione reductase GLR1 transcription by decreasing glutathione and D-erythroascorbic acid and increasing pyruvate. The CCP1-deficient mutant maintains steady-state levels of methylglyoxal. CCP1/EAPX1 double disruptants show severe growth defects due to the D-erythroascorbic acid and glutathione depletion because of pyruvate overaccumulation. CCP1-deficient and CCP1/EAPX1 double-knockout mutants show more hyphal growth than the wild-type	742669	
1.11.1.5	physiological function	cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense. The enzyme in intermembrane space functions primarily as a mitochondrial H2O2 sensing and signaling protein in yeast cells. Ccp1 H2O2 sensing and signaling regulate Sod2 activity to control superoxide levels. Respiration-derived H2O2 is removed principally by mitochondrial catalase Cta1, which is regulated in a H2O2-dependent manner by Ccp1, overview	-, 725070	
1.11.1.5	physiological function	disruption of the cytochrome c peroxidase gene causes a decrease of the membrane NADH peroxidase activity, impairs the resistance of growing culture to exogenous hydrogen peroxide and hampers aerobic growth. The mutation does not affect the activity or oxygen affinity of the respiratory chain, or the kinetics of cytochrome d reduction. Cytochrome c peroxidase does not terminate the cytochrome bc1 branch of Zymomonas mobilis	-, 743248	
1.11.1.5	physiological function	electron transfer	702250	
1.11.1.5	physiological function	increased copy number of CCP1 on chromosome XI activates respiratory metabolism and decreases pyruvate levels in an aneuploid sake yeast	-, 765121	
1.11.1.5	physiological function	involvement of ZmCytC in the aerobic respiratory chain via the cytochrome bc1 complex in addition to the previously proposed direct interaction with ubiquinol and its contribution to protection against oxidative stress	725756	
1.11.1.5	physiological function	the parasite's peroxidase LmP helps to protect the parasite from oxidative stress. LmP is a heme peroxidase that catalyzes the peroxidation of mitochondrial cytochrome c	726385