Coordination chemistry and function of the catalytic metal ion in liver alcohol dehydrogenase

This publication has 26 references indexed in Scilit:

• Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives.
  Proceedings of the National Academy of Sciences, 1983
• Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analog
  Biochemistry, 1983
• Kinetics and mechanisms of the recombination of Zn2+, Co2+, and Ni2+ with the metal-depleted catalytic site of horse liver alcohol dehydrogenase
  Journal of Inorganic Biochemistry, 1983
• Isolierung und Charakterisierung von Glycerin-Dehydrogenase ausBacillus megaterium
  Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
• Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type.
  Proceedings of the National Academy of Sciences, 1981
• Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(2+) and competition with zinc(2+) and cadmium(2+) ions
  Biochemistry, 1981
• Probes of Mechanism and Transition-State Structure in the Alcohol Dehydrogenase Reactio
  Critical Reviews in Biochemistry, 1981
• Active site-specifically reconstituted nickel(II) horse liver alcohol dehydrogenase: Optical spectra of binary and ternary complexes with coenzymes, coenzyme analogues, substrates, and inhibitors
  Journal of Inorganic Biochemistry, 1981
• Active site-specific reconstituted copper(II) horse liver alcohol dehydrogenase: A biological model for type 1 Cu2+ and its changes upon ligand binding and conformational transitions
  Journal of Inorganic Biochemistry, 1980
• Site‐Specific Substituted Cobalt(II) Horse Liver Alcohol Dehydrogenases
  European Journal of Biochemistry, 1979