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...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2019-05, Vol.55 (41), p.5777-578
Hauptverfasser:	Mahajan, Mukesh, Ravula, Thirupathi, Prade, Elke, Anantharamaiah, G. M, Ramamoorthy, Ayyalusamy
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Beschreibung
Zusammenfassung:	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