PMID: 3769916Oct 1, 1986Paper

Studies on the reaction mechanism of general acyl-CoA dehydrogenase. Determination of selective isotope effects in the dehydrogenation of butyryl-CoA

European Journal of Biochemistry
B PohlS Ghisla

Abstract

The kinetic properties of general acyl-CoA dehydrogenase from pig kidney have been investigated using normal butyryl-CoA as well as an alpha-deutero, beta-deutero- and perdeutero-butyryl-CoA. In turnover catalysis, isotope effects of 2, 3.6, and 9 were found respectively. In the reductive half reaction the isotope effects were 2.5, 14, and 28 for the same substrates, and 21 for (2R,3R)-(2,3-D2)butyryl-CoA. No intermediates are apparent during the reduction of oxidized enzyme to the presumed complex of reduced enzyme and crotonyl-CoA. The results are interpreted as indicating a high degree of concertedness during the rupture of the alpha and beta C-H bonds. They are compatible with a mechanism in which simultaneously the alpha-hydrogen is abstracted as a proton, while the beta-hydrogen is transferred to the oxidized flavin as a hydride.

References

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Citations

Jul 20, 2002·Archives of Biochemistry and Biophysics·Teresa R LammMarian T Stankovich
Jun 22, 2007·The Journal of Organic Chemistry·Steven O MansoorabadiHung-wen Liu
Jan 20, 2004·European Journal of Biochemistry·Sandro Ghisla, Colin Thorpe
Apr 15, 1989·European Journal of Biochemistry·S Ghisla, V Massey
Aug 24, 2004·Protein Science : a Publication of the Protein Society·Mireia Garcia-VilocaJiali Gao
Dec 8, 2004·Journal of Molecular Biology·Lise Pedersen, Anette Henriksen
Apr 1, 1988·Archives of Biochemistry and Biophysics·S M Lau, C Thorpe
Dec 3, 2014·Applied and Environmental Microbiology·Jin ZhangWolfgang Buckel
Aug 8, 2001·Archives of Biochemistry and Biophysics·I Rudik, C Thorpe
Jun 9, 2005·Journal of the American Chemical Society·Jiaquan WuPeter J Tonge
Dec 21, 2006·Biochemistry·K Sudhindra RaoFrank E Frerman

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