Cytochrome c peroxidase (CcP)

Cytochrome c peroxidase is a heme-containing mitochondrial enzyme found primarily in yeast. It catalyzes the reduction of hydrogen peroxide to water using ferrocytochrome c as an electron donor, thereby detoxifying hydrogen peroxide and protecting cells from oxidative damage[1][6]. The enzyme plays a central role in maintaining cellular redox balance by eliminating toxic radical molecules produced during metabolism[8]. Structurally, it consists mainly of α-helices with a single heme group at its active site. Key residues such as His175, Asn235, and Trp191 are critical for its catalytic mechanism[1][2]. In addition to its enzymatic activity, cytochrome c peroxidase also functions as a mitochondrial H₂O₂ sensor and signaling protein, helping regulate ROS levels within the organelle[3]. While it is not considered a direct therapeutic target or associated with specific human diseases, it serves as an important model for understanding biological electron transfer processes and oxidative stress responses.

Other names

CcPcytochrome-c peroxidasemitochondrial cytochrome c peroxidaseCCP1 (in yeast)