Copper(II)‐substituted horse liver alcohol dehydrogenase: Structure of the minor species

FEBS Letters

Zeppezauer, Michael¹  Fey, Frunk²  Formicka, Grazyna¹  Hüttermann, Jürgen² 

[1] Department 12.4 Biochemistry, University of Saarland, D-6600 Saarbruecken, Germany;Dept. 3.6 Biophysics, University of Saarland, D-6650 Hamburg/Saar, Germany

关键词: Alcohol dehydrogenase;    Copper(II)-protein;    EPR;    CD;    Absorption spectra;   

DOI  :  10.1016/0014-5793(92)80747-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown