The natural flavorprotein electron acceptor of trimethylamine 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/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.
D001419:Bacteria / Q000201:enzymology; D004227:Dithionite; D004578:Electron Spin Resonance Spectroscopy; D005486:Flavin Mononucleotide; D005420:Flavoproteins; D007700:Kinetics; D008744:Methylamines; D010084:Oxidation-Reduction; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism; D013053:Spectrophotometry
D005420:Flavoproteins; D008744:Methylamines; D004227:Dithionite; D005486:Flavin Mononucleotide; D010089:Oxidoreductases, N-Demethylating; C023186:trimethylamine dehydrogenase