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Detection of domain motion in NADPH-cytochrome P450 oxidoreductase through polarization anisotropy measurements
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Detection of domain motion in NADPH-cytochrome P450 oxidoreductase through polarization anisotropy measurements
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Detection of domain motion in NADPH-cytochrome P450 oxidoreductase through polarization anisotropy measurements
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Paper
Detection of domain motion in NADPH-cytochrome P450 oxidoreductase through polarization anisotropy measurements
2017
Overview
Conformational transitions between closed and open states in the NADPH-cytochrome P450 oxidoreductase (POR) play a critical role in its electron-transport function. In this study, we determined rotational diffusion coefficients of the EDANS fluorophore attached to the cytosolic POR construct lacking the N-terminal transmembrane region. We identified two dynamic modes, slow and fast, which are interpreted as the rotational diffusion of POR as a whole and the local domain motion, respectively. Timescale of the local rotational diffusion component suggests that it may correspond to the transient opening of the fully oxidized POR structure.
Publisher
Cold Spring Harbor Laboratory Press,Cold Spring Harbor Laboratory
Subject
