Ontology highlight
ABSTRACT:
SUBMITTER: Mahajan M
PROVIDER: S-EPMC7467500 | biostudies-literature | 2019 May
REPOSITORIES: biostudies-literature
Mahajan Mukesh M Ravula Thirupathi T Prade Elke E Anantharamaiah G M GM Ramamoorthy Ayyalusamy A
Chemical communications (Cambridge, England) 20190501 41
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. ...[more]