Conformational States of Cytochrome P450 Oxidoreductase Evaluated by Förster Resonance Energy Transfer Using Ultrafast Transient Absorption Spectroscopy.
作者信息
Kovrigina Elizaveta A, Pattengale Brian, Xia Chuanwu, Galiakhmetov Azamat R, Huang Jier, Kim Jung-Ja P, Kovrigin Evgenii L
机构信息
Biochemistry Department, Medical College of Wisconsin , Milwaukee, Wisconsin 53226, United States.
Chemistry Department, Marquette University , P.O. Box 1881, Milwaukee, Wisconsin 53201, United States.
出版信息
Biochemistry. 2016 Nov 1;55(43):5973-5976. doi: 10.1021/acs.biochem.6b00623. Epub 2016 Oct 19.
Abstract
NADPH-cytochrome P450 oxidoreductase (CYPOR) was shown to undergo large conformational rearrangements in its functional cycle. Using a new Förster resonance energy transfer (FRET) approach based on femtosecond transient absorption spectroscopy (TA), we determined the donor-acceptor distance distribution in the reduced and oxidized states of CYPOR. The unmatched time resolution of TA allowed the quantitative assessment of the donor-acceptor FRET, indicating that CYPOR assumes a closed conformation in both reduced and oxidized states in the absence of the redox partner. The described ultrafast TA measurements of FRET with readily available red-infrared fluorescent labels open new opportunities for structural studies in chromophore-rich proteins and their complexes.
摘要
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