The structure of formaldehyde-inhibited xanthine oxidase determined by 35 GHz [super 2]H ENDOR spectroscopy

Authors :: Shanmugam, Muralidharan
Bo Zhang
McNaughton, Rebecca L.
Kinney, R. Adam
Hille, Russ
Hoffman, Brian M.
Source :: Journal of the American Chemical Society. Oct 13, 2010, Vol. 132 Issue 40, 14015-14017
Publication Year :: 2010
Abstract: The formaldehyde-inhibited Mo(V) state of xanthine oxidase (I) is analyzed. [super 1]H and [super 2]H ENDOR spectra of xanthine oxidase(C[super 1,2][H.sub.2]O) in [H.sub.2]O/[D.sub.2]O buffer have shown that the active-site structure of xanthine oxidase contains a C[H.sub.2]O adduct of Mo(V) in the form of a four-membered ring with S and O linking the C to Mo and have ruled out a direct Mo-C bond.

Subjects :: Enzyme inhibitors -- Chemical properties
Enzyme inhibitors -- Structure
Enzyme inhibitors -- Spectra
Formaldehyde -- Chemical properties
Oxidases -- Chemical properties
Oxidases -- Structure
Chemistry

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