Literature DB >> 207689

The natural flavorprotein electron acceptor of trimethylamine dehydrogenase.

D J Steenkamp, M Gallup.   

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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Year:  1978        PMID： 207689

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  12 in total

1.  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.

Authors:  J Basran; M J Sutcliffe; R Hille; N S Scrutton
Journal:  Biochem J       Date:  1999-07-15       Impact factor: 3.857

2.  Flavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: a study of the protein environment around the N1 of the flavin isoalloxazine.

Authors:  M Mewies; L C Packman; F S Mathews; N S Scrutton
Journal:  Biochem J       Date:  1996-07-01       Impact factor: 3.857

3.  6-Hydroxypseudooxynicotine Dehydrogenase Delivers Electrons to Electron Transfer Flavoprotein during Nicotine Degradation by Agrobacterium tumefaciens S33.

Authors:  Rongshui Wang; Jihong Yi; Jinmeng Shang; Wenjun Yu; Zhifeng Li; Haiyan Huang; Huijun Xie; Shuning Wang
Journal:  Appl Environ Microbiol       Date:  2019-05-16       Impact factor: 4.792

4.  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.

Authors:  D J Steenkamp; H Beinert
Journal:  Biochem J       Date:  1982-11-01       Impact factor: 3.857

5.  Localization of the major dehydrogenases in two methylotrophs by radiochemical labeling.

Authors:  A A Kasprzak; D J Steenkamp
Journal:  J Bacteriol       Date:  1983-10       Impact factor: 3.490

6.  Electron transfer flavoprotein from pig liver mitochondria. A simple purification and re-evaluation of some of the molecular properties.

Authors:  M Husain; D J Steenkamp
Journal:  Biochem J       Date:  1983-02-01       Impact factor: 3.857

7.  Characterization of the baiH gene encoding a bile acid-inducible NADH:flavin oxidoreductase from Eubacterium sp. strain VPI 12708.

Authors:  C V Franklund; S F Baron; P B Hylemon
Journal:  J Bacteriol       Date:  1993-05       Impact factor: 3.490

8.  Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 2. Kinetic studies on the intramolecular electron transfer in trimethylamine and dimethylamine dehydrogenase.

Authors:  D J Steenkamp; H Beinert
Journal:  Biochem J       Date:  1982-11-01       Impact factor: 3.857

Review 9.  Molecular genetics of the genus Paracoccus: metabolically versatile bacteria with bioenergetic flexibility.

Authors:  S C Baker; S J Ferguson; B Ludwig; M D Page; O M Richter; R J van Spanning
Journal:  Microbiol Mol Biol Rev       Date:  1998-12       Impact factor: 11.056

10.  A single arginine residue is required for the interaction of the electron transferring flavoprotein (ETF) with three of its dehydrogenase partners.

Authors:  Antony R Parker
Journal:  Mol Cell Biochem       Date:  2003-12       Impact factor: 3.396
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