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Proton nmr investigation of the active site of cobalt ii substituted liver alcohol dehydrogenase ec 1.1.1.1



Proton nmr investigation of the active site of cobalt ii substituted liver alcohol dehydrogenase ec 1.1.1.1



Journal of the American Chemical Society 106(6): 1826-1830



The pH dependence of the 1H NMR spectra of active-site specifically substituted Co(II) horse liver alcohol dehydrogenase and its complexes with NAD and NADH are reported. The 1H NMR signals of the cysteine and the histidine ligands are well shifted from the diamagnetic position. The .delta.-NH of histidine 67 probably deprotonates with a pKa of 9.0 .+-. 0.2; in the complex with NAD the same group exhibits a pH-dependent shift without deprotonation with a pKa of 8.3 .+-. 0.2. The complex with NADH is pH independent up to pH 9.3. Both the 1H NMR and near-IR spectra indicate that no major change in the coordination sphere of the catalytic metal ion occurs upon binding coenzyme. The results suggest the participation in catalysis of groups not considered in previously proposed mechanisms.

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Accession: 006215739

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