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

Date

1999

Authors

Trebeck, Katherine
Golding, Bernard
Radom, Leo

Journal Title

Journal ISSN

Volume Title

Publisher

American Chemical Society

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.

Description

Keywords

Keywords: acetaldehyde; cobamamide; diol dehydratase; ethylene glycol; hydrolyase; unclassified drug; article; catalysis; enzyme activity; enzyme substrate complex; proton transport

Citation

Source

Journal of the American Chemical Society

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1021/ja990209g

Restricted until

2037-12-31