J Biol Chem. 1978 Jun 25;253(12):4086-9.

The natural flavorprotein electron acceptor of trimethylamine dehydrogenase.

Abstract

The isolation and partial characterization of a flavoprotein which functions as the electron acceptor of trimethylamine dehydrogenase (EC 1.5.99.7) from a methylotrophic bacterium is described. It has a molecular weight of 77,000 and is composed of two dissimilar subunits. All preparations examined contained only 1 mol of FAD/mol of the flavoprotein. Trimethylamine dehydrogenase, in the presence of trimethylamine or dithionite, reduced the flavoprotein to a stable anionic semiquinone form. No evidence for the participation of the fully reduced flavoprotein in catalysis could be obtained.

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Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 1. The influence of substrate binding to reduced trimethylamine dehydrogenase on the intramolecular electron transfer between its prosthetic groups. [Biochem J. 1982]
Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 1. The influence of substrate binding to reduced trimethylamine dehydrogenase on the intramolecular electron transfer between its prosthetic groups.
Steenkamp DJ, Beinert H. Biochem J. 1982 Nov 1; 207(2):233-9.
Electron transfer flavoprotein from Methylophilus methylotrophus: properties, comparison with other electron transfer flavoproteins, and regulation of expression by carbon source. [J Bacteriol. 1986]
Electron transfer flavoprotein from Methylophilus methylotrophus: properties, comparison with other electron transfer flavoproteins, and regulation of expression by carbon source.
Davidson VL, Husain M, Neher JW. J Bacteriol. 1986 Jun; 166(3):812-7.
Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis. [Biochem J. 1978]
Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis.
Steenkamp DJ, Singer TP. Biochem J. 1978 Feb 1; 169(2):361-9.
Review Electron transfer in trimethylamine dehydrogenase and electron-transferring flavoprotein. [Biochem Soc Trans. 1999]
Review Electron transfer in trimethylamine dehydrogenase and electron-transferring flavoprotein.
Scrutton NS, Basran J, Wilson EK, Chohan KK, Jang MH, Sutcliffe MJ, Hille R. Biochem Soc Trans. 1999 Feb; 27(2):196-201.
Review Trimethylamine dehydrogenase and electron transferring flavoprotein. [Subcell Biochem. 2000]
Review Trimethylamine dehydrogenase and electron transferring flavoprotein.
Scrutton NS, Sutcliffe MJ. Subcell Biochem. 2000; 35:145-81.

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Cited by 10 PubMed Central articles

Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex. [Biochem J. 1999]
Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex.
Basran J, Sutcliffe MJ, Hille R, Scrutton NS. Biochem J. 1999 Jul 15; 341 ( Pt 2):307-14.
Review Molecular genetics of the genus Paracoccus: metabolically versatile bacteria with bioenergetic flexibility. [Microbiol Mol Biol Rev. 1998]
Review Molecular genetics of the genus Paracoccus: metabolically versatile bacteria with bioenergetic flexibility.
Baker SC, Ferguson SJ, Ludwig B, Page MD, Richter OM, van Spanning RJ. Microbiol Mol Biol Rev. 1998 Dec; 62(4):1046-78.
Flavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: a study of the protein environment around the N1 of the flavin isoalloxazine. [Biochem J. 1996]
Flavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: a study of the protein environment around the N1 of the flavin isoalloxazine.
Mewies M, Packman LC, Mathews FS, Scrutton NS. Biochem J. 1996 Jul 1; 317 ( Pt 1):267-72.

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