Open AccessAn overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions
Author(s) -
Zinhle Edith Chiliza,
José MartínezOyanedel,
Khajamohiddin Syed
Publication year - 2020
Publication title -
biophysical reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.766
H-Index - 39
eISSN - 1867-2469
pISSN - 1867-2450
DOI - 10.1007/s12551-020-00749-7
Subject(s) - ferredoxin , cytochrome p450 , monooxygenase , cytochrome , redox , biochemistry , heme , electron transfer , biology , enzyme , chemistry , computational biology , photochemistry , organic chemistry
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.