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- W2080388698 abstract "Perturbed angular correlation spectra on horse liver alcohol dehydrogenase, measured on 111Cd inserted specifically in the catalytic site, have been obtained under various conditions. Spectra have been obtained in the pH range 6–9 and in the presence of coenzyme and/or pyrazole or trifluoroethanol No ionization at the metal site could be detected between pH 6 and 9, irrespectively of whether NAD+ is present or not. From this we conclude that a water molecule ligated to Cd(II) must have a pK of ionization higher than 9.5. Both coenzyme, pyrazole and trifluoroethanol affect the spectra of Cd incorporated in the catalytic site of alcohol dehydrogenase. The interpretation of the present data is consistent with a four coordinated, nearly tetrahedral metal geometry, both with and without the coenzyme bound to the enzyme. The effect of the coenzyme on the metal coordination can best be explained by a reduction of the two cysteine metal bond lengths. From an analysis of the data we conclude that both pyrazole and trifluoroethanol enter as a fifth ligand not displacing the solvent ligand to the metal." @default.
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- W2080388698 date "1982-01-01" @default.
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- W2080388698 title "Structural information concerning the catalytic metal site in horse liver alcohol dehydrogenase, obtained by perturbed angular correlation spectroscopy on 111Cd" @default.
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- W2080388698 doi "https://doi.org/10.1016/s0020-1693(00)85039-2" @default.
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