Redox Partners: Function Modulators of Bacterial P450 Enzymes

• Published in: Trends in microbiology (Regular ed.) Vol. 28; no. 6; pp. 445 - 454
• Main Authors: Li, Shengying, Du, Lei, Bernhardt, Rita
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.06.2020; Elsevier Science Ltd
• Subjects: Bacteria; Cytochrome; Cytochrome P450; cytochrome P450 enzymes; Cytochromes P450; Electron transfer; ferredoxin; ferredoxin reductase; Mode of action; Modulators; protein–protein interactions; redox partners; Reductases; Selectivity; Substrates; protein–protein interactions; ferredoxin; electron transfer; redox partners; ferredoxin reductase; cytochrome P450 enzymes
• ISSN: 0966-842X; 1878-4380
• DOI: 10.1016/j.tim.2020.02.012

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. Ubiquitous P450s catalyze various oxidative reactions towards an enormous number of substrates. Bacterial P450s in soluble forms represent the most diverse subset with great application value and potential.In the conventional notion, redox partners are auxiliary proteins influencing electron transfer efficiency and product distribution. Lately, growing evidence has demonstrated that redox partners can endow their paired P450s with novel functionalities and may have more unexplored physiological roles.Bacterial redox partners can form various combinations to serve different P450s in vivo. This flexibility may be important for the host microorganisms to deal with ever-changing environments.Selection and engineering of redox partners for an optimized P450–redox partner interaction interface will become an important strategy for the improvement of industrially relevant P450 catalysts.