Open AccessProbing membrane enhanced protein–protein interactions in a minimal redox complex of cytochrome-P450 and P450-reductase
Author(s) -
Mukesh Mahajan,
Thirupathi Ravula,
Elke Prade,
G.M. Anantharamaiah,
Ayyalusamy Ramamoorthy
Publication year - 2019
Publication title -
chemical communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.837
H-Index - 333
eISSN - 1364-548X
pISSN - 1359-7345
DOI - 10.1039/c9cc01630a
Subject(s) - redox , cytochrome p450 , chemistry , cytochrome p450 reductase , reductase , enzyme , biochemistry , cytochrome c , cytochrome , coenzyme q – cytochrome c reductase , mitochondrion , organic chemistry
Investigating the interplay in a minimal redox complex of cytochrome-P450 and its reductase is crucial for understanding cytochrome-P450's enzymatic activity. Probing the hotspots of dynamic structural interactions using NMR revealed the engagement of loop residues from P450-reductase to be responsible for the enhanced affinity of CYP450 towards its obligate redox partner.