The coordination chemistry of the catalytic zinc ion in alcohol dehydrogenase studied by ab initio quantum chemical calculations
- 15 November 1994
- journal article
- research article
- Published by Wiley in International Journal of Quantum Chemistry
- Vol. 52 (5) , 1229-1243
- https://doi.org/10.1002/qua.560520508
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- pKa of zinc-bound water and nucleophilicity of hydroxo-containing species. Ab initio calculations on models for zinc enzymesInorganic Chemistry, 1990
- Influence of anions and pH on the conformational change of horse liver alcohol dehydrogenase induced by binding of oxidized nicotinamide adenine dinucleotide: binding of chloride to the catalytic metal ionBiochemistry, 1986
- Liver Alcohol DehydrogenasCritical Reviews in Biochemistry, 1986
- Investigation of intermediates and transition states in the catalytic mechanisms of active site substituted cobalt(II), nickel(II), zinc,(II), and cadmium(II) horse liver alcohol dehydrogenasesBiochemistry, 1982
- Ligand Binding to the blue copper center of horse liver alcohol dehydrogenaseFEBS Letters, 1981
- Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolutionJournal of Molecular Biology, 1981
- Probes of Mechanism and Transition-State Structure in the Alcohol Dehydrogenase ReactioCritical Reviews in Biochemistry, 1981
- Unified Mechanism for Proton‐Transfer Reactions Affecting the Catalytic Activity of Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1980
- Crystallography of liver alcohol dehydrogenase complexed with substratesJournal of Molecular Biology, 1978
- pH, isotope, and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenaseBiochemistry, 1977