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

David M. Smith, Bernard T. Golding, Leo Radom*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    61 Citations (Scopus)

    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 with 18O-labeling experiments and thus overcomes important shortcomings in previously proposed mechanisms.

    Original languageEnglish
    Pages (from-to)5700-5704
    Number of pages5
    JournalJournal of the American Chemical Society
    Volume121
    Issue number24
    DOIs
    Publication statusPublished - 23 Jun 1999

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