Probing membrane enhanced protein-protein interactions in a minimal redox complex of cytochrome-P450 and P450-reductase

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 res...

Full description

Saved in:
Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2019-05, Vol.55 (41), p.5777-578
Main Authors: Mahajan, Mukesh, Ravula, Thirupathi, Prade, Elke, Anantharamaiah, G. M, Ramamoorthy, Ayyalusamy
Format: Article
Language:English
Subjects:
Animals
Cytochrome P-450 Enzyme System - chemistry
Cytochrome P-450 Enzyme System - metabolism
Humans
Models, Molecular
NADPH-Ferrihemoprotein Reductase - chemistry
NADPH-Ferrihemoprotein Reductase - metabolism
Nuclear Magnetic Resonance, Biomolecular - methods
Oxidation-Reduction
Protein Interaction Mapping - methods
Protein Interaction Maps
Rabbits
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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. Investigating the interplay in a minimal redox complex of cytochrome-P450 and its reductase is crucial for understanding cytochrome-P450's enzymatic activity.
ISSN:1359-7345
1364-548X
DOI:10.1039/c9cc01630a