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The structure of formaldehyde-inhibited xanthine oxidase determined by 35 GHz 2H ENDOR spectroscopy.
Autor:
Shanmugam M; Chemistry Department, Northwestern University, Evanston, Illinois 60208-3113, USA., Zhang B, McNaughton RL, Kinney RA, Hille R, Hoffman BM
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2010 Oct 13; Vol. 132 (40), pp. 14015-7.
Autor:
R. Adam Kinney, Bo Zhang, Rebecca L. McNaughton, Russ Hille, Muralidharan Shanmugam, Brian M. Hoffman
Publikováno v:
Journal of the American Chemical Society. 132:14015-14017
The formaldehyde-inhibited Mo(V) state of xanthine oxidase (I) has been studied for four decades, yet it has not proven possible to distinguish unequivocally among the several structures proposed for this form. The uniquely large isotropic hyperfine
Publikováno v:
Journal of the American Chemical Society. 123(11)
Xanthine oxidase is a molybdenum-containing enzyme that catalyzes the hydroxylation of xanthine and a wide variety of other aromatic heterocycles. In the course of the reaction with xanthine and substrates such as 2-hydroxy-6-methylpurine (HMP), the