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Trimethylamine dehydrogenase structure

Lim, L.W., et al. Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4 A resolution. J. Biol. Chem. 261 15140-15146, 1986. [Pg.65]

Steenkamp, D. J., Mclntire, W., and Kenney, W. C., 1978, Structure of the covalently bound coenzyme of trimethylamine dehydrogenase. Evidence for a 6-substituted flavin. J. Biol. Ghent. 253 2818n2824. [Pg.72]

The foeus of this chapter is the soluble electron transfer complex formed between the nieotinamide-independent trimethylamine dehydrogenase (TMADH) and eleetron transferring flavoprotein (ETF). Recent studies of this physiological electron transfer complex have provided invaluable insight into (i) the mechanisms of inter and intraprotein electron transfer between flavin and Fe/S centers, (ii) the role of dynamics in interprotein electron transfer and (hi) quantum meehanieal mechanisms for the cleavage of substrate C-H bonds and the subsequent transfer of reducing equivalents to flavin redox centers. Brief mention is made of early structural and cofactor analyses for this redox system, but more detailed accounts of this work can be found in earlier reviews on the subjeet (e.g. Steenkamp and Mathews, 1992). [Pg.148]

Mathews, F. S., Trickey, P., Barton, J. D., and Chen, Z.-W., 1996, Crystal structures of recombinant wild-type and a C30A mutant trimethylamine dehydrogenase from Methylophilus WjAi, in Flavins and Flavoproteins (K. Stevenson, V. Massey, and C. H. Williams, eds.). University of Calgary Press, Calgary, pp. 873-876. [Pg.179]

Steenkamp, D. J., and Mathews, F. S., 1992, The biochemical properties and structure of trimethylamine dehydrogenase, in Chemistry and Biochemistry of Flavoenzymes, Volume II (F. Muller, ed.), CRC Press, Boca Raton, pp. 395n423. [Pg.181]

Other members of this family that have been structurally determined by X-ray diffraction include formate dehydrogenase (FDH), trimethylamine oxidase (TMAO), dissimilatory nitrate reductase(NAP), and most recently, arsenite oxidase (AsO). Only the distinctive points of their structures will be briefly described here. [Pg.513]


See other pages where Trimethylamine dehydrogenase structure is mentioned: [Pg.265]    [Pg.265]    [Pg.40]    [Pg.188]    [Pg.784]    [Pg.72]    [Pg.146]    [Pg.179]    [Pg.179]    [Pg.784]    [Pg.40]    [Pg.1343]    [Pg.73]    [Pg.239]    [Pg.2668]    [Pg.164]    [Pg.448]    [Pg.472]    [Pg.5570]    [Pg.223]    [Pg.630]    [Pg.223]    [Pg.5569]    [Pg.61]    [Pg.372]    [Pg.2661]   
See also in sourсe #XX -- [ Pg.266 ]




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