Expression, purification, and functional reconstitution of ¹⁹F-labeled cytochrome b5 in peptide nanodiscs for NMR studies.

ABSTRACT: Microsomal cytochrome b5 (cytb5) is a membrane-bound protein capable of donating the second electron to cytochrome P450s (cytP450s) in the cytP450s monooxygenase reactions. Recent studies have demonstrated the importance of the transmembrane domain of cytb5 in the interaction with cytP450 by stabilizing its monomeric structure. While recent NMR studies have provided high-resolution insights into the structural interactions between the soluble domains of ~16-kDa cytb5 and ~57-kDa cytP450 in a membrane environment, there is need for studies to probe the residues in the transmembrane region as well as to obtain intermolecular distance constraints to better understand the very large size cytb5-cytP450 complex structure in a near native membrane environment. In this study, we report the express

SUBMITTER: Bai J 

PROVIDER: S-EPMC7050362 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature