Journal
ACS CATALYSIS
Volume 8, Issue 11, Pages 9992-10003Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.8b02913
Keywords
cytochrome P450 enzymes; redox partners; electron transfer; protein protein interaction; ferredoxin; ferredoxin reductase
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Funding
- Shandong Provincial Natural Science Foundation [ZR2017ZB0207, ZR2016CB10]
- National Natural Science Foundation of China [81741155, 31422002, 21472204, 31570030]
- Qilu Youth Scholar Startup Funding of Shandong University
- Chinese Academy of Sciences [QYZDB-SSW-SMC042]
- National Postdoctoral Innovative Talent Support Program [BX20180325]
- China Postdoctoral Science Foundation [188229]
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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 O-2 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.
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