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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1986
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Pohl, Brigitte
Raichle, Thomas
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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.x
Zusammenfassung

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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570 Biowissenschaften, Biologie
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ISO 690POHL, 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.x
BibTex
@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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