Abstract
Cytochrome P450 monooxygenases (CYPs/P450s) are heme-thiolate proteins that are ubiquitously present in organisms, including non-living entities such as viruses. With the exception of self-sufficient P450s, all other P450 enzymes need electrons to perform their enzymatic activity and these electrons are supplied by P450 redox proteins. Different types of P450 redox proteins can be found in organisms and are classified into different classes. Bacterial P450s (class I) receive electrons from ferredoxins which are iron-sulfur cluster proteins. The presence of more than one copy and different types of ferredoxins within a bacterial species poses fundamental questions about the selectivity of P450s and ferredoxins in relation to each other. Apart from transferring electrons, ferredoxins have also been found to modulate P450 functions. Achieving an understanding of the interaction between ferredoxins and P450s is required to harness their biotechnological potential for designing a universal electron transfer protein. A brief overview of factors playing a role in ferredoxin and P450 interactions is presented in this review article.
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Acknowledgments
The authors want to thank Barbara Bradley, Pretoria, South Africa, for English language editing. The authors also thank the Proceedings of the National Academy of Sciences of the United States of America (PNAS, USA) for granting permission to use Figure 4 panel A, from the article: Sevrioukova IF, Li H, Zhang H, Peterson JA, Poulos TL (1999) Structure of a cytochrome P450–redox partner electron-transfer complex, Proceedings of the National Academy of Sciences 96:1863-1868.
Funding
Khajamohiddin Syed expresses sincere gratitude to the National Research Foundation (NRF), South Africa, for a research grant (Grant No. 114159). Zinhle Edith Chiliza thanks the NRF, South Africa, for a DST-NRF Innovation Master’s Scholarship for the year 2019 (Grant No. 117182).
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Chiliza, Z.E., Martínez-Oyanedel, J. & Syed, K. An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions. Biophys Rev 12, 1217–1222 (2020). https://doi.org/10.1007/s12551-020-00749-7
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DOI: https://doi.org/10.1007/s12551-020-00749-7