Hydrogen transfer in catalysis by adenosylcobalamin-dependent diol dehydratase
Abstract
Studies [Bachovchin, W. W., et al. (1978) Biochemistry 17, 2218] of the mechanism of inactivation of adenosylcobalamin-dependent diol dehydratase have led to the development of a general method to describe the kinetics of a reaction pathway containing a reservoir of mobile hydrogen. Analysis by this method of catalytic rate measurements for mixtures of 1,2-propanediol and 1, 1-dideuterio-1,2-propanediol supports a mechanism involving an intermediate with three equivalent hydrogens, in which hydrogen transfer from this intermediate to product is the major rate-contributing step. Other results using tritium as a trace label [Essenberg, M. K., et al. (1971) J. Am. Chem. Soc. 93, 1242] are considered in light of these deuterium isotope studies.
Additional Information
© 1979 American Chemical Society. Received October 2, 1978; revised manuscript received February 13, 1979. This is Contribution No. 5878. This research was supported by National Institutes of Health Grant GM-10218.Additional details
- Eprint ID
- 57098
- DOI
- 10.1021/bi00580a013
- Resolver ID
- CaltechAUTHORS:20150429-150734315
- GM-10218
- NIH
- Created
-
2015-04-30Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Church Laboratory of Chemical Biology
- Other Numbering System Identifier
- 5878