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
- 1 January 1980
- journal article
- research article
- Published by Elsevier in Journal of Inorganic Biochemistry
- Vol. 12 (3), 241-252
- https://doi.org/10.1016/s0162-0134(00)80205-6
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Site‐Specific Substituted Cobalt(II) Horse Liver Alcohol DehydrogenasesEuropean Journal of Biochemistry, 1979
- EPR studies on the blue copper protein, rusticyaninFEBS Letters, 1978
- X-ray crystal structure analysis of plastocyanin at 2.7 Å resolutionNature, 1978
- Spectroscopic studies and a structural model for blue copper centers in proteins.Proceedings of the National Academy of Sciences, 1976
- Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolutionJournal of Molecular Biology, 1976
- Plantacyanin from spinachFEBS Letters, 1975
- Conversion of metallothionein into Cu-thionein, the possible low molecular weight form of neonatal hepatic mitochondrocupreinFEBS Letters, 1974
- Models for copper-protein interaction based on solution and crystal structure studiesCoordination Chemistry Reviews, 1974
- On the state of copper in the blue protein umecyaninFEBS Letters, 1971
- The Assay and Specific Activity of Crystalline Alcohol Dehydrogenase of Horse Liver.Acta Chemica Scandinavica, 1957