Probing protein-protein and protein-substrate interactions in the dynamic membrane-associated ternary complex of cytochromes P450, b5, and reductase

Katherine A Gentry; G M Anantharamaiah; Ayyalusamy Ramamoorthy

doi:10.1039/c9cc05904k

Probing protein-protein and protein-substrate interactions in the dynamic membrane-associated ternary complex of cytochromes P450, b₅, and reductase

Chem Commun (Camb). 2019 Nov 18;55(89):13422-13425. doi: 10.1039/c9cc05904k. Epub 2019 Oct 22.

Authors

Katherine A Gentry¹, G M Anantharamaiah², Ayyalusamy Ramamoorthy¹

Affiliations

¹ Biophysics and Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, University of Michigan, Ann Arbor, MI 48109-1055, USA. ramamoor@umich.edu kagentry@umich.edu.
² Department of Medicine, UAB Medical Center, Birmingham, Alabama 35294, USA.

Abstract

Cytochrome P450 (cytP450) interacts with two redox partners, cytP450 reductase and cytochrome-b₅, to metabolize substrates. Using NMR, we reveal changes in the dynamic interplay when all three proteins are incorporated into lipid nanodiscs in the absence and presence of substrates.

MeSH terms

Cytochrome P-450 Enzyme System / chemistry*
Cytochrome P-450 Enzyme System / metabolism
Cytochromes b5 / chemistry*
Cytochromes b5 / metabolism
Humans
Models, Molecular
NADPH-Ferrihemoprotein Reductase / chemistry*
NADPH-Ferrihemoprotein Reductase / metabolism
Oxidation-Reduction
Substrate Specificity

Substances

Cytochromes b5
Cytochrome P-450 Enzyme System
NADPH-Ferrihemoprotein Reductase

Abstract

MeSH terms

Substances

Grants and funding