The natural flavorprotein electron acceptor of trimethylamine dehydrogenase.
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چکیده
منابع مشابه
The Natural Flavoprotein Electron Acceptor of Trimeihylamine Dehydrogenase*
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/m01 of the flavoprotein. Trimethylamine dehydrogenase, in the presenc...
متن کاملFlavin radicals, conformational sampling and robust design principles in interprotein electron transfer: the trimethylamine dehydrogenase-electron-transferring flavoprotein complex.
TMADH (trimethylamine dehydrogenase) is a complex iron-sulphur flavoprotein that forms a soluble electron-transfer complex with ETF (electron-transferring flavoprotein). The mechanism of electron transfer between TMADH and ETF has been studied using stopped-flow kinetic and mutagenesis methods, and more recently by X-ray crystallography. Potentiometric methods have also been used to identify ke...
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The interactions between proteins and biological membranes are important for drug development, but remain notoriously refractory to structural investigation. We combine non-denaturing mass spectrometry (MS) with molecular dynamics (MD) simulations to unravel the connections among co-factor, lipid, and inhibitor binding in the peripheral membrane protein dihydroorotate dehydrogenase (DHODH), a k...
متن کاملStructure of the Covalently Bound Coenzyme of Trimethylamine Dehydrogenase
Trimethylamine dehydrogenase contains an unusual covalently bound coenzyme, which has been isolated in the form of a flavin peptide and converted to a novel type of aminoacyl flavin (Steenkamp, D. J., Kenney, W. C., and Singer, T. P. (1978) J. Biol. Chem. 253, 2812-2817). The present paper presents evidence that the aminoacyl coenzyme is a thioether substituted at C-6 of the flavin ring of FMN,...
متن کاملA novel type of covalently bound coenzyme in trimethylamine dehydrogenase.
Bacterial trimethylamine dehydrogenase contains a covalently bound yellow coenzyme, the properties of which distinguish it from all known riboflavin, pyridoxine, and pteridine derivatives. A pure dodecapeptide containing the covalently linked coenzyme has been isolated from tryptic-chymotryptic digests. Treatment with aminopeptidase M converts it to a ninhydrin-positive aminoacyl coenzyme, whic...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34685-9