Advanced Understanding of the Electron Transfer Pathway of Cytochrome P450s. (28th December 2020)

• Record Type: Journal Article
• Authors: Chen, Chun‐Chi; Min, Jian; Zhang, Lilan; Yang, Yu; Yu, Xuejing; Guo, Rey‐Ting
• Is Part Of: Chembiochem. Volume 22:Number 8(2021)
• Page Start: 1317
• Page End: 1328
• Publication Date: 2020-12-28
• Subjects: catalytic reactions -- cytochromes -- electron transport -- protein structure -- self-sufficient P450; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.202000705
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Cytochrome P450s are heme‐thiolate enzymes that participate in carbon source assimilation, natural compound biosynthesis and xenobiotic metabolism in all kingdoms of life. P450s can catalyze various reactions by using a wide range of organic compounds, thus exhibiting great potential in biotechnological applications. The catalytic reactions of P450s are driven by electron equivalents that are sourced from pyridine nucleotides and delivered by cognate or matching redox partners (RPs). The electron transfer (ET) route from RPs to P450s involves one or more redox center‐containing domains. As the rate of ET is one of the main determinants of P450 efficacy, an in‐depth understanding of the P450 ET pathway should increase our knowledge of these important enzymes and benefit their further applications. Here, the various P450 RP systems along with current understanding of their ET routes will be reviewed. Notably, state‐of‐the‐art structural studies of the two main types of self‐sufficient P450 will also be summarized. Abstract : Versatile P450s catalyze various reactions upon acquiring electrons from redox partners. Electrons transferred from the cofactor to heme are of central importance to P450 action, but the route electrons travel remains unveiled. This issue might be probed under the guidance of recent structural studies of self‐sufficient P450s.