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Arch Biochem Biophys. 2021 Dec 15;714:109076. doi: 10.1016/j.abb.2021.109076. Epub 2021 Oct 31.

Binding of cytochrome P450 27C1, a retinoid desaturase, to its accessory protein adrenodoxin.

Archives of biochemistry and biophysics

Sarah M Glass, Stephany N Webb, F Peter Guengerich

Affiliations

  1. Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232-0146, United States.
  2. Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232-0146, United States. Electronic address: [email protected].

PMID: 34732331 PMCID: PMC8629852 DOI: 10.1016/j.abb.2021.109076

Abstract

Of the 57 human cytochrome P450 (P450) enzymes, seven are mitochondrial: 11A1, 11B1, 11B2, 24A1, 27A1, 27B1, and 27C1. Mitochondrial P450s utilize an electron transport system with adrenodoxin (Adx) and NADPH-adrenodoxin reductase (AdR). AdR reduces Adx, which then transfers electrons to the P450. The interactions between proteins in the mitochondrial P450 system are largely driven by electrostatic interactions, though the specifics vary depending on the P450. Unlike other mitochondrial P450s, the interaction between P450 27C1, a retinoid 3,4-desaturase expressed in the skin, and Adx remains largely uncharacterized. In this work, we utilized an Alexa Fluor 488 C

Copyright © 2021 Elsevier Inc. All rights reserved.

Keywords: Adrenodoxin; CYP; Cytochrome P450; Mass spectrometry; NADPH-Adrenodoxin reductase; P450; Protein cross-linking; Protein-protein interaction

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