Toward a consistent mechanism for diol dehydratase catalyzed reactions: an application of the partial-proton-transfer concept

Katherine Trebeck, Bernard Golding, Leo Radom

    Research output: Contribution to journalArticle

    Abstract

    Ab initio molecular orbital theory has been used to study the reactions catalyzed by the B12-dependent enzyme diol dehydratase. The calculations show that a pathway involving the 1,2-shift of a hydroxyl group is greatly facilitated by partial proton transfer to the migrating oxygen. These results suggest a conceptually simple mechanism for the rearrangement whose reaction rate is consistent with experiment. The inclusion of a gem-diol intermediate in the proposed pathway is in accordance with18O-labeling experiments and thus overcomes important shortcomings in previously proposed mechanisms.
    Original languageEnglish
    Pages (from-to)5700-5704
    JournalJournal of the American Chemical Society
    Volume121
    DOIs
    Publication statusPublished - 1999

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