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- W4247651812 abstract "Unexpectedly, the isotope effect of ethanol-1-Τ as a substrate of yeast alcohol dehydrogenase, increases with rising temperature from k H /k T = 3.2 at 5 —15°C to 3.8—4.7 at 20 —35 °C. This suggests a change of the rate controlling step as proposed by MÜLLER-HILL and WALLENFELS, who investigated the temperature dependence of the activation energies in this temperature range. A comparison of the affinities of propanol and butanol with the isotope effects of the corresponding tritium labelled compounds (propanol-1-Τ 6.7 at 25 °C, butanol-1-Τ 6.8 at 25 °C) supports the proposal, that during substrate binding, there must be a direct interaction between the enzyme complex and hydrogen which is removed in the reaction. These influences are less pronounced for the ethanol homologues which are bound less tightly to the enzyme. Therefore the H transfering step proper gives a greater contribution to the overall experimental isotope effect." @default.
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- W4247651812 date "1966-06-01" @default.
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- W4247651812 title "Untersuchungen zur Reaktion der Alkoholdehydrogenase mit Tritium-markierten Substraten" @default.
- W4247651812 doi "https://doi.org/10.1515/znb-1966-0609" @default.
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