scholarly article | Q13442814 |
P2093 | author name string | M. Zeppezauer | |
H. Dietrich | |||
H. H. Ruf | |||
W. Maret | |||
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X-ray crystal structure analysis of plastocyanin at 2.7 Å resolution | Q28314769 | ||
Site-Specific Substituted Cobalt(II) Horse Liver Alcohol Dehydrogenases. Preparation and Characterization in Solution, Crystalline and Immobilized State | Q30409267 | ||
Spectroscopic studies and a structural model for blue copper centers in proteins | Q34999583 | ||
EPR studies on the blue copper protein, rusticyanin: a protein involved in Fe2+ oxidation at pH 2.0 in Thiobacillus ferro-oxidans | Q39212963 | ||
A crystallographic model for azurin a 3 A resolution | Q39614759 | ||
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Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution | Q39990970 | ||
Active-site-specific reconstituted cobalt(II) horse-liver alcohol dehydrogenase. Changes of the spectra of the substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde and of the catalytic cobalt ion upon ternary complex formation with NADH and 1,4,5,6- | Q40258906 | ||
Differences between Alcohol Dehydeogenases. Structural Properties and Evolutionary Aspects | Q40750032 | ||
Plantacyanin from spinach | Q45329836 | ||
Conversion of metallothionein into Cu-thionein, the possible low molecular weight form of neonatal hepatic mitochondrocuprein | Q47357156 | ||
On the state of copper in the blue protein umecyanin. | Q50971256 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | biochemistry | Q7094 |
alcohol oxidoreductase | Q4713306 | ||
inorganic chemistry | Q11165 | ||
ligand binding | Q61659151 | ||
P304 | page(s) | 241-252 | |
P577 | publication date | 1980-06-01 | |
P1433 | published in | Journal of Inorganic Biochemistry | Q3186919 |
P1476 | title | 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 | |
P478 | volume | 12 |
Q70177042 | Active site-specifically reconstituted nickel(II) horse liver alcohol dehydrogenase: optical spectra of binary and ternary complexes with coenzymes, coenzyme analogues, substrates, and inhibitors |
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Q41892824 | Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids |
Q42167238 | Yeast copper-thionein can reconstitute the Japanese-lacquer-tree (Rhus vernicifera) laccase from the Type 2-copper-depleted enzyme via a direct copper(I)-transfer mechanism |