On the mechanism of hydrogen transfer by nicotinamide coenzymes and some dehydrogenases

David Laurie*, Edward Lucas, Derek C. Nonhebel, Colin J. Suckling, John C. Walton

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The course of the oxidation of 2,2-dimethylcyclopropylmethanol and 2,2,3,3-tetramethylcyclopropylmethanol by horse liver alcohol dehydrogenase and NAD+ has been investigated. In neither case were ring opened products detected which, in agreement with previous observations, provides no evidence for the intermediacy of radicals in these reactions. The stability of several substituted cyclopropylalkyl radicals has been investigated by e.s.r. spectroscopy and the results are discussed with respect to cyclopropane-containing probes of the mechanism of oxidation of lactate dehydrogenase.

Original languageEnglish
Pages (from-to)1035-1045
Number of pages11
JournalTetrahedron
Volume42
Issue number4
DOIs
Publication statusPublished - 1 Jan 1986

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