Redox Partners: Function Modulators of Bacterial P450 Enzymes.

State Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, China; Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, Shandong 266237, China. Electronic address: lishengying@sdu.edu.cn. State Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, China; Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, Shandong 266101, China. Department of Biochemistry, Campus B2.2, Saarland University, D-66123 Saarbrücken, Germany. Electronic address: ritabern@mx.uni-saarland.de.

Trends in microbiology. 2020;(6):445-454
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Abstract

The superfamily of cytochrome P450 monooxygenases (P450s) is widespread in all kingdoms of life. Functionally versatile P450s are extensively involved in diverse anabolic and catabolic processes. P450s require electrons to be transferred by redox partners (RPs) for O2 activation and substrate monooxygenation. Unlike monotonic eukaryotic cytochrome P450 reductases, bacterial RP systems are more diverse and complicated. Recent studies have demonstrated that the type, the amount, the combination, and the mode of action of bacterial RPs can affect not only the catalytic rate and product distribution but also the type and selectivity of P450 reactions. These results are leading to a novel opinion that RPs not only function as auxiliary electron transfer proteins but are also important P450 function modulators.

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Publication Type : Review

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