Kinetics and mechanisms of the recombination of Zn2+, Co2+, and Ni2+ with the metal-depleted catalytic site of horse liver alcohol dehydrogenase.

[1]  S. H. Koenig,et al.  Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(II) and competition with zinc(II) and cadmium(II) ions. , 1981, Biochemistry.

[2]  W. Maret,et al.  Active site-specifically reconstituted nickel(II) horse liver alcohol dehydrogenase: optical spectra of binary and ternary complexes with coenzymes, coenzyme analogues, substrates, and inhibitors. , 1981, Journal of inorganic biochemistry.

[3]  W. Maret,et al.  Site-specific substituted cobalt(II) horse liver alcohol dehydrogenases. Preparation and characterization in solution, crystalline and immobilized state. , 1979, European journal of biochemistry.

[4]  R. Marks,et al.  A kinetic study of the reconstitution of azurin from Cu(II) and the apoprotein. , 1979, Archives of biochemistry and biophysics.

[5]  D. McMillin,et al.  A detailed analysis of the charge-transfer bands of a blue copper protein. Studies of the nickel(II), manganese(II), and cobalt(II) derivatives of azurin , 1979 .

[6]  C. Lochmüller,et al.  Kinetics and mechanism of dissociation of zinc ion from carbonic anhydrase. , 1978, Bioinorganic chemistry.

[7]  A. Sytkowski,et al.  Cobalt exchange in horse liver alcohol dehydrogenase. , 1978, Biochemistry.

[8]  K. K. Brito,et al.  Kinetics of formation and dissociation of metallocarboxypeptidases. , 1978, Bioinorganic chemistry.

[9]  G. Rotilio,et al.  The binding of copper ions to copper-free bovine superoxide dismutase. Kinetic aspects. , 1978, The Biochemical journal.

[10]  H. Eklund,et al.  Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution. , 1976, Journal of molecular biology.

[11]  F. Ng,et al.  The interaction of cobalt (II) complexes with bovine apocarbonic anhydrase B. , 1975, Bioinorganic chemistry.

[12]  Chasteen Nd,et al.  Electron paramagnetic resonance studies of the structure and metal ion exchange kinetics of vanadyl(IV) bovine carbonic anhydrase. , 1974 .

[13]  K. Williams,et al.  Kinetics of formation and dissociation of manganese-bovine carbonic anhydrase B. , 1974, Journal of the American Chemical Society.

[14]  A. Finazzi-Agro’,et al.  The role of copper binding in the conformation of stellacyanin , 1974 .

[15]  R. G. Wilkins Substitution processes in simple and complicated metal complexes , 1973 .

[16]  B. Vallee,et al.  Differential chemical reactivities of zinc in horse liver alcohol dehydrogenase. , 1970, Biochemistry.

[17]  B. Vallee,et al.  Zinc isotope exchange in horse liver alcohol dehydrogenase. , 1969, Biochemistry.

[18]  J. Sturtevant,et al.  The kinetics of the binding of zinc(II) by apocarbonic anhydrase , 1968 .

[19]  Å. Åkeson On the zinc content of horse liver alcohol dehydrogenase. , 1964, Biochemical and biophysical research communications.

[20]  S. Lindskog Effects of pH and inhibitors on some properties related to metal binding in bovine carbonic anhydrase. , 1963, The Journal of biological chemistry.

[21]  B. Vallee,et al.  Metallocarboxypeptidases: stability constants and enzymatic characteristics. , 1961, The Journal of biological chemistry.

[22]  R. Martin,et al.  The Association of Divalent Cations with Glutathione1 , 1959 .

[23]  K. Dalziel,et al.  The Assay and Specific Activity of Crystalline Alcohol Dehydrogenase of Horse Liver. , 1957 .