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

Chem Commun (Camb). 2019 May 16;55(41):5777-5780. doi: 10.1039/c9cc01630a.

Abstract

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.

MeSH terms

  • 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

Substances

  • Cytochrome P-450 Enzyme System
  • NADPH-Ferrihemoprotein Reductase