A dynamic understanding of cytochrome P450 structure and function through solution NMR.

ABSTRACT: Many economically important biosyntheses incorporate regiospecific and stereospecific oxidations at unactivated carbons. Such oxidations are commonly catalyzed by cytochrome P450 monooxygenases, heme-containing enzymes that activate molecular oxygen while selectively binding and orienting the substrate for reaction. Despite the plethora of P450-catalyzed reactions, the P450 fold is highly conserved, and static structures are often insufficient for characterizing conformational states that contribute to specificity. High-resolution solution nuclear magnetic resonance (NMR) offers insights into dynamic processes and conformational changes that are required of a P450 in order to attain the combination of specificity and efficiency required for these reactions.

SUBMITTER: Pochapsky TC 

PROVIDER: S-EPMC8215082 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature