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

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

Katherine A. Gentry,^a G. M. Anantharamaiah^b and Ayyalusamy Ramamoorthy

Author affiliations

^a Biophysics and Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, University of Michigan, Ann Arbor, MI 48109-1055, USA
E-mail: ramamoor@umich.edu, kagentry@umich.edu

^b Department of Medicine, UAB Medical Center, Birmingham, Alabama, 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.

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Article information

DOI: https://doi.org/10.1039/C9CC05904K
Article type: Communication
Submitted: 29 Jul 2019
Accepted: 24 Sep 2019
First published: 02 Oct 2019

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Chem. Commun., 2019,55, 13422-13425

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

K. A. Gentry, G. M. Anantharamaiah and A. Ramamoorthy, Chem. Commun., 2019, 55, 13422 DOI: 10.1039/C9CC05904K

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