Copper(II)‐substituted horse liver alcohol dehydrogenase: Structure of the minor species
- 31 August 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 309 (1) , 92-96
- https://doi.org/10.1016/0014-5793(92)80747-5
Abstract
Oxygen treatment of horse liver alcohol dehydrogenase EE isoenzyme substituted with Cu(II) at the catalytic site leads to bleaching with concomitant reduction to Cu(I) of‐90% of total Cu(II). The Cu(II) of the remaining ‘minor species’ cannot be reduced nor does it interact with exogenous ligands, e.g. 2‐mercaploethanol, imidazole, purazole, or the azide ions. The EPR spectrum is axial with a super‐hyperfine splitting of 15.6G indicating binding of one nitrogen atom to Cu(II). These data as well as the energies and intensities of the absorption and CD spectra suggest the Cu(II) ion of the minor species to be located in the catalytic site of HLADH in a position and geometry different from that of the major species.Keywords
This publication has 13 references indexed in Scilit:
- X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosaJournal of Molecular Biology, 1991
- Electronic absorption and EPR spectroscopy of copper alcohol dehydrogenase: pink, violet and green forms at a Type 1 copper center analogBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Resonance Raman spectroscopy of blue copper proteins: ligand and coenzyme effects in copper(II)-substituted liver alcohol dehydrogenaseJournal of the American Chemical Society, 1986
- Blue copper proteins. The copper site in azurin from Alcaligenes denitrificansJournal of the American Chemical Society, 1986
- Structure of oxidized poplar plastocyanin at 1·6 Å resolutionJournal of Molecular Biology, 1983
- Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analogBiochemistry, 1983
- An EPR study of the blue copper center in horse liver alcohol dehydrogenaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Ligand Binding to the blue copper center of horse liver alcohol dehydrogenaseFEBS Letters, 1981
- Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(2+) and cobalt(2+) ionsBiochemistry, 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 transitionsJournal of Inorganic Biochemistry, 1980