Updating the Paradigm: Redox Partner Binding and Conformational Dynamics in Cytochromes P450.

ABSTRACT: This Account summarizes recent findings centered on the role that redox partner binding, allostery, and conformational dynamics plays in cytochrome P450 proton coupled electron transfer. P450s are one of Nature's largest enzyme families and it is not uncommon to find a P450 wherever substrate oxidation is required in the formation of essential molecules critical to the life of the organism or in xenobiotic detoxification. P450s can operate on a remarkably large range of substrates from the very small to the very large, yet the overall P450 three-dimensional structure is conserved. Given this conservation of structure, it is generally assumed that the basic catalytic mechanism is conserved. In nearly all P450s, the O₂ O-O bond must be cleaved heterolytically enabling one oxygen a

SUBMITTER: Poulos TL 

PROVIDER: S-EPMC8959394 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature