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pubmed-article:10612596pubmed:abstractTextProcessing of trans-2-phenylcyclopropylmethanols 5 and 6 by the monocopper/tyrosine radical enzyme galactose oxidase led to mechanism-based inactivation with a partition ratio, (k(cat) + k(inact))/k(inact), of approximately 1 and a primary deuterium isotope effect, k(inact(H))/k(inact(D)), of 3.2. The data are consistent with a radical mechanism for galactose oxidase with a short lived ketyl radical anion intermediate.lld:pubmed
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pubmed-article:10612596pubmed:articleTitleProbing the radical mechanism of galactose oxidase using an ultrafast radical probe.lld:pubmed
pubmed-article:10612596pubmed:affiliationDepartment of Chemistry, University of Oregon, Eugene 97403-1253, USA.lld:pubmed
pubmed-article:10612596pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10612596pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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