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The action of coenzyme B₁₂-dependent diol dehydratase on 3,3,3-trifluoro-1,2-propanediol results in elimination of all the fluorides with formation of acetaldehyde

Lookup NU author(s): Emeritus Professor Bernard Golding

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Abstract

© 2024 The Author(s). Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.3,3,3-Trifluoro-1,2-propanediol undergoes complete defluorination in two distinct steps: first, the conversion into 3,3,3-trifluoropropionaldehyde catalyzed by adenosylcobalamin (coenzyme B12)-dependent diol dehydratase; second, non-enzymatic elimination of all three fluorides from this aldehyde to afford malonic semialdehyde (3-oxopropanoic acid), which is decarboxylated to acetaldehyde. Diol dehydratase accepts 3,3,3-trifluoro-1,2-propanediol as a relatively poor substrate, albeit without significant mechanism-based inactivation of the enzyme during catalysis. Optical and electron paramagnetic resonance (EPR) spectra revealed the steady-state formation of cob(II)alamin and a substrate-derived intermediate organic radical (3,3,3-trifluoro-1,2-dihydroxyprop-1-yl). The coenzyme undergoes Co-C bond homolysis initiating a sequence of reaction by the generally accepted pathway via intermediate radicals. However, the greater steric size of trifluoromethyl and especially its negative impact on the stability of an adjacent radical centre compared to a methyl group has implications for the mechanism of the diol dehydratase reaction. Nevertheless, 3,3,3-trifluoropropionaldehyde is formed by the normal diol dehydratase pathway, but then undergoes non-enzymatic conversion into acetaldehyde, probably via 3,3-difluoropropenal and malonic semialdehyde.

Publication metadata

Author(s): Mori K, Golding BT, Toraya T

Publication type: Article

Publication status: Published

Journal: Journal of Biochemistry

Year: 2024

Volume: 176

Issue: 3

Pages: 245-254

Print publication date: 01/09/2024

Online publication date: 11/07/2024

Acceptance date: 20/06/2024

ISSN (print): 0021-924X

ISSN (electronic): 1756-2651

Publisher: Oxford University Press

URL: https://doi.org/10.1093/jb/mvae047

DOI: 10.1093/jb/mvae047

PubMed id: 38987935

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