Detection of domain motion in NADPH-cytochrome P450 oxidoreductase through polarization anisotropy measurements
Detection of domain motion in NADPH-cytochrome P450 oxidoreductase through polarization anisotropy measurements
ABSTRACT 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.
Kovrigin Evgenii L、Xia Chuanwu、Kim Jung-Ja P.、Kovrigina Elizaveta A
Chemistry Department, Marquette UniversityBiochemistry Department, Medical College of WisconsinBiochemistry Department, Medical College of WisconsinBiochemistry Department, Medical College of Wisconsin||Chemistry Department, Marquette University
生物化学生物物理学分子生物学
Kovrigin Evgenii L,Xia Chuanwu,Kim Jung-Ja P.,Kovrigina Elizaveta A.Detection of domain motion in NADPH-cytochrome P450 oxidoreductase through polarization anisotropy measurements[EB/OL].(2025-03-28)[2025-05-29].https://www.biorxiv.org/content/10.1101/178426.点此复制
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