Publikation: Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA
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The kinetic properties of general acyl-CoA dehydrogenase from pig kidney have been investigated using normal butyryl-CoA as well as a α-deutero, β-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 α and β C-H bonds. They are compatible with a mechanism in which simultaneously the α-hydrogen is abstracted as a proton, while the β-hydrogen is transferred to the oxidized flavin as a hydride.
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POHL, Brigitte, Thomas RAICHLE, Sandro GHISLA, 1986. Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA. In: European Journal of Biochemistry. 1986, 160(1), pp. 109-115. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1986.tb09946.xBibTex
@article{Pohl1986Studi-7325, year={1986}, doi={10.1111/j.1432-1033.1986.tb09946.x}, title={Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA}, number={1}, volume={160}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={109--115}, author={Pohl, Brigitte and Raichle, Thomas and Ghisla, Sandro} }
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