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Distribution of reducing equivalents on xanthine oxidase molecules and the rates of the intramolecular electron-transfer reactions (Short Communication)
Authors:Robert C. Bray   David J. Lowe     Michael J. Barber
Affiliation:School of Molecular Sciences, University of Sussex, Falmer, Brighton BN1 9QJ, U.K.
Abstract:When xanthine oxidase turns over 1-methylxanthine aerobically at pH8.2, the time-sequence in development of its electron-paramagnetic-resonance signals is not primarily due to slow intramolecular reactions among its centres. It derives instead from gross differences in electron distribution within enzyme molecules reduced by the substrate in comparison with those that have subsequently been partly reoxidized by one-electron reaction with oxygen.
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