Probing 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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom