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Electronic structure contribution to reactivity in pyranopterin Mo enzymes is presented and discussed. This is accomplished by relating spectroscopic studies of relevant model compounds with those of the enzymes. This has contributed to a greater understanding of how the pyranopterin dithiolene functions in catalysis, and has led to an enhanced understanding of how electronic structure controls reactivity in sulfite oxidase, xanthine oxidase, CO dehydrogenase, DMSO reductase and MOSC family proteins.

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