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

Lookup NU author(s): Emeritus Professor Bernard Golding


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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.

Publication metadata

Author(s): Smith DM, Golding BT, Radom L

Publication type: Article

Publication status: Published

Journal: Journal of the American Chemical Society

Year: 1999

Volume: 121

Issue: 24

Pages: 5700-5704

Print publication date: 23/06/1999

ISSN (print): 0002-7863

ISSN (electronic): 1520-5126

Publisher: American Chemical Society


DOI: 10.1021/ja990209g


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