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Proceedings Paper

Proof Of Forster Energy Transfer Between Fad And Fmn In Cytochrome P450 Reductase By Time-Resolved Red-Edge Spectroscopy.
Author(s): P I.H Bastiaens; P J.M Bonants; A van Hoek; F Muller; A J.W.G Visser
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Paper Abstract

By use of steady state and time-resolved fluorescence techniques Forster energy transfer between the cofactors, FAD and FMN, in cytochrome-P450 reductase is observed. Red-edge spectroscopy allowed us to assign the actual rate constant of transfer as apparent in the anisotropy decay of the holoenzyme. The same approach was used in biflavinyl compounds entrapped in polymethylmetacrylate. As anticipated the fluorescence depolarisation of this system showed a great similarity with the enzyme system. From the results the interflavin distance in the enzyme was estimated between 1.6 and 2.4 nm.

Paper Details

Date Published: 24 June 1988
PDF: 6 pages
Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); doi: 10.1117/12.945398
Show Author Affiliations
P I.H Bastiaens, Agricultural University (The Netherlands)
P J.M Bonants, Agricultural University (The Netherlands)
A van Hoek, Agricultural University (The Netherlands)
F Muller, Agricultural University (The Netherlands)
A J.W.G Visser, Agricultural University (The Netherlands)

Published in SPIE Proceedings Vol. 0909:
Time-Resolved Laser Spectroscopy in Biochemistry
Joseph R. Lakowicz, Editor(s)

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