Premium
Copper(II)‐substituted horse liver alcohol dehydrogenase: Structure of the minor species
Author(s) -
Formicka Grazyna,
Zeppezauer Michael,
Fey Frunk,
Hüttermann Jürgen
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80747-5
Subject(s) - chemistry , catalysis , copper , azide , imidazole , alcohol , absorption spectroscopy , alcohol dehydrogenase , horse , electron paramagnetic resonance , medicinal chemistry , stereochemistry , crystallography , photochemistry , inorganic chemistry , organic chemistry , nuclear magnetic resonance , biology , physics , quantum mechanics , paleontology
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.