Redox Partners in Proximity to CYP51B1 of Mycobacterium Tuberculosis: An in Silico Approach Confirming in Vitro Elec-tron Transfer

Abstract

Enzymes of the cytochrome P450 (CYP) superfamily of heme-thiolate proteins are found in most biological species from all five kingdoms. The discovery of a prokaryotic CYP51 was an exciting discovery in the P450 field because of the soluble nature of CYP51B1. The different sorts of redox partners interactions utilized in cytochrome P450 system are depicted. The redox reactions are a family of reactions that are concerned with the transfer of electrons between species. The 3D structure of Ferredoxin1(Fd1), Ferredoxin2(Fd2) and FerredoxinReductase (Fdr) from Mycobacterium tuberculosis have not been solved and published in any online databases. Data mining has been done using two online databases, tuberculist and PDB. Then, homology modeling was performed using two different softwares and verify 3D was used to evaluate the models. Docking analysis to compare redox partner protein models for distances and interactions to CYP51B1. As a conclusion, 3D structures of redox partners Fd1, Fd2 and Fdr were successfully built. Their electron transfer process in proximity to the heme domain was elucidated for a better understanding of CYP51 interactions with its redox partner proteins complementing experimental results