Abstract
This chapter reviews studies by electron paramagnetic resonance (EPR) on the nature and reactions of the molybdenum center of xanthine oxidase. Xanthine oxidase is the most extensively studied of the molybdenum-containing enzymes. EPR has been essential for investigating other centers in the enzyme xanthine oxidase. Apart from molybdenum, each subunit of xanthine oxidase has a flavin molecule and two Fe-S centres that participate in the electron transfer reactions. The molybdenum in the resting, untreated enzyme is normally in the diamagnetic 6-valent state. After reduction with substrates or dithionite, a proportion of the metal is detectable by EPR as molybdenum(V); the rest presumably existing as diamagnetic molybdenum(IV) and molybdenum(VI). One of the most important methods for generating the molybdenum(V) signals in a form suitable for investigation by EPR has been rapid freezing and has been indispensable for studying a number of features of the catalytic mechanism.
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