An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions
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REVIEW
An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions Zinhle Edith Chiliza 1
&
José Martínez-Oyanedel 2
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Khajamohiddin Syed 1
Received: 9 June 2020 / Accepted: 28 August 2020 # International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2020
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. Keywords Cytochrome P450 monooxygenase . Ferredoxins . Interactions . Redox potentials . Evolution . Heme . Iron-sulfur cluster
Introduction Cytochrome P450 monooxygenases (CYPs/P450s) represent one of the largest and oldest gene super-families found in all biological kingdoms (Nelson 2018), including non-living entities such as viruses (Lamb et al. 2019). P450s were named after their unusual spectrum with a peak of absorbance at 450 nm owing to the presence of heme-moiety (Klingenberg 1958). P450s activate molecular oxygen (White and Coon 1980) for the oxidative metabolism of a great variety of organic molecules (Bernhardt 2006; Fasan 2012; Isin and Guengerich 2007; Le-Huu et al. 2015; Sono et al. 1996; Syed et al. 2013). The primary reaction catalyzed by P450s is monooxygenation; i.e., one oxygen atom obtained from
* Khajamohiddin Syed [email protected] 1
Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa 3886, South Africa
2
Laboratorio de Biofísica Molecular, Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción, Chile
molecular oxygen is inserted into a substrate while the second oxygen atom undergoes reduction to water (White and Coon 1980). P450s need two electrons to perform their enzymatic reaction (White and Coon 1980). P450s receive these electrons from P450 redox proteins, with the exception of the so-called self-sufficient P450s that are fused to different types of P450
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