EXAFS analysis of xanthine oxidase complexes with alloxanthine, violapterin, and 6-pteridylaldehyde
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منابع مشابه
The Inhibition of Xanthine Oxidase in Vitro by Trace Amounts of Z-ascorbic Acid by Philip Feigelson
For many years it has been known that numerous compounds can act as inhibitors of xanthine oxidase in vitro. This has been demonstrated for such diverse substances as cyanide (I), copper (Z), oxidized p-aminophenol (3), pyrogallol (4), 6-pteridylaldehyde (5), Antabuse (6), and numerous flavonoids (7). Few, if any, of the above inhibitors can be considered as being present and normally participa...
متن کاملThe inhibition of xanthine oxidase by flavonoids and related compounds.
Investigations of the inhibition of the activity of xanthine oxidase in vitro have yielded a number of substances which have been reported to exert marked inhibitory actions at low concentrations. Among these are p-aminophenol in its oxidized form (l), pyrogallol (a), bromoacetophenone (3)) 6-pteridylaldehyde (4)) and 6-hydroxymethylpterin (5). An examination of the structures of these compound...
متن کاملResonance-enhanced Raman scattering from the molybdenum center of xanthine oxidase.
The molybdenum center of xanthine oxidase has been examined by resonance Raman spectroscopy. Making use of the long-wavelength absorption of the reduced molybdenum center in complex with violapterin (the product of enzymic action of lumazine), resonance Raman spectra were obtained using laser excitation at 676.4 nm. Several internal vibrational modes of violapterin were found to be resonance-en...
متن کاملRecent mechanistic studies of xanthine oxidase.
Introduction The molybdenum-containing hydroxylases constitute one of the three major categories of mononuclear molybdenum enzymes. In comparison with other biological hydroxylation systems they are unique in that they utilize water rather than dioxygen as the ultimate source of the oxygen atom incorporated into product, and generate rather than consume reducing equivalents in the course of tur...
متن کاملCrystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus.
Xanthine dehydrogenase (XDH), a complex molybdo/iron-sulfur/flavoprotein, catalyzes the oxidation of hypoxanthine to xanthine followed by oxidation of xanthine to uric acid with concomitant reduction of NAD+. The 2.7 A resolution structure of Rhodobacter capsulatus XDH reveals that the bacterial and bovine XDH have highly similar folds despite differences in subunit composition. The NAD+ bindin...
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