title: Peroxidase activity enhancement of horse cytochrome c by dimerization.
abstract: The peroxidase activity of horse cytochrome c was enhanced by its dimerization, where its Compound III (oxy-form) and Compound I (oxoferryl porphyrin π-cation radical) species were detected in the reactions with hydrogen peroxide and meta-chloroperbenzoic acid, respectively. These results show that oligomeric cytochrome c can contribute as a proapoptotic conformer by the increased peroxidase activity.
authors.affiliation: Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
authors.forename: Zhonghua
authors.initials: Z
authors.lastname: Wang
authors.forename: Takashi
authors.initials: T
authors.lastname: Matsuo
authors.forename: Satoshi
authors.initials: S
authors.lastname: Nagao
authors.forename: Shun
authors.initials: S
authors.lastname: Hirota
mesh_terms: D000818:Animals; D045304:Cytochromes c / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D006736:Horses / Q000378:metabolism*; D007700:Kinetics; D055503:Protein Multimerization
chemical_list: D045304:Cytochromes c