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J Biol Chem, Vol. 275, Issue 17, 12546-12552, April 28, 2000
From the The electron-transferring flavoprotein (ETF) from
Methylophilus methylotrophus (sp.
W3A1) exhibits unusual oxidation-reduction properties and can only be reduced to the level of the semiquinone under most circumstances (including turnover with its physiological reductant, trimethylamine dehydrogenase (TMADH), or reaction with strong reducing reagents such as sodium dithionite). In the present study, we demonstrate that ETF can be reduced fully to its hydroquinone form both enzymatically and chemically when it is in complex with TMADH. Quantitative titration of the TMADH·ETF protein complex with
sodium dithionite shows that a total of five electrons are taken up by
the system, indicating that full reduction of ETF occurs within the
complex. The results indicate that the oxidation-reduction properties
of ETF are perturbed upon binding to TMADH, a conclusion further
supported by the observation of a spectral change upon formation of the
TMADH·ETF complex that is due to a change in the environment of the
FAD of ETF. The results are discussed in the context of ETF undergoing
a conformational change during formation of the TMADH·ETF electron
transfer complex, which modulates the spectral and oxidation-reduction
properties of ETF such that full reduction of the protein can take place.
Formation of W3A1 Electron-transferring
Flavoprotein (ETF) Hydroquinone in the Trimethylamine
Dehydrogenase·ETF Protein Complex*
,
Department of Medical Biochemistry, Ohio
State University, Columbus, Ohio 43210 and the
§ Department of Biochemistry, University of Leicester,
Adrian Building, University Road,
Leicester LE1 7RH, United Kingdom
*
This work was supported by National Institutes of Health
Grant GM 58481 (to R. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence and reprint requests should be
addressed. Tel.: 614-292-3545; Fax: 614-292-4118; E-mail:
hille.1@osu.edu.
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