Conformational States of Cytochrome P450 Oxidoreductase Evaluated by Förster Resonance Energy Transfer Using Ultrafast Transient Absorption Spectroscopy

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 distribu...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 2016-11, Vol.55 (43), p.5973-5976
Main Authors: Kovrigina, Elizaveta A, Pattengale, Brian, Xia, Chuanwu, Galiakhmetov, Azamat R, Huang, Jier, Kim, Jung-Ja P, Kovrigin, Evgenii L
Format: Article
Language:English
Subjects:
Crystallography, X-Ray
Fluorescence Resonance Energy Transfer
NADPH-Ferrihemoprotein Reductase - chemistry
Protein Conformation
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/acs.biochem.6b00623