Kinetics and mechanisms of the recombination of Zn2+, Co2+, and Ni2+ with the metal-depleted catalytic site of horse liver alcohol dehydrogenase.
暂无分享,去创建一个
[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 .