Document Type

Article

Language

eng

Format of Original

4 p.

Publication Date

11-1-2016

Publisher

American Chemical Society

Source Publication

Biochemistry

Source ISSN

0006-2960

Original Item ID

DOI: 10.1021/acs.biochem.6b00623; PMID: 27741572

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.

Comments

Accepted version. Biochemistry, Vol. 55, No. 43 (November 1, 2016): 5973-5976. DOI. © American Chemical Society 2016. Used with permission.

Available for download on Wednesday, November 01, 2017

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