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- W2894479533 endingPage "10003" @default.
- W2894479533 startingPage "9992" @default.
- W2894479533 abstract "Cytochrome P450 enzymes are highly diversified biocatalysts associated with steroid biosynthesis, xenobiotic metabolism, biosynthesis of natural products, and industrial oxidation reactions. A typical P450 catalytic cycle requires sequential transfer of two electrons from NAD(P)H to the heme-iron reactive center for O2 activation. For the most abundant bacterial Class I P450 systems, this important process is usually mediated by two redox partner proteins including an FAD-containing ferredoxin reductase (FdR) and a small iron–sulfur protein, ferredoxin (Fdx). However, it is often unclear which pair of Fdx and FdR among multiple redox partners is the optimal one for a specific Class I P450 enzyme. To address this important but underexplored question, herein, a reaction matrix network with 16 Fdxs, 8 FdRs, and 6 P450s (against 7 substrates) was constituted. By analyzing the reactivity profiles of 896 P450 reactions, together with phylogenetic analysis, redox potential measurements, structural simulations, and Fdx-P450 molecular docking, we provide important mechanistic insights into the recognition and interactions between bacterial Class I P450 enzymes and redox partners." @default.
- W2894479533 created "2018-10-05" @default.
- W2894479533 creator A5015641840 @default.
- W2894479533 creator A5031924369 @default.
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- W2894479533 creator A5052773815 @default.
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- W2894479533 creator A5071932485 @default.
- W2894479533 creator A5077601572 @default.
- W2894479533 creator A5079450677 @default.
- W2894479533 creator A5086195615 @default.
- W2894479533 creator A5087950344 @default.
- W2894479533 date "2018-09-28" @default.
- W2894479533 modified "2023-10-15" @default.
- W2894479533 title "Mechanistic Insights into Interactions between Bacterial Class I P450 Enzymes and Redox Partners" @default.
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