Structural properties of the zinc site in Cu,Zn-superoxide dismutase; Perturbed angular correlation of gamma ray spectroscopy on the Cu, 111Cd-superoxide dismutase derivative |
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Authors: | R. Bauer I. Demeter V. Hasemann J.T. Johansen |
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Affiliation: | x. The Niels Bohr Institute, University of Copenhagen, DK4000 Roskilde, Denmark;4. Central Research Institute for Physics, H1525 Budapest, Hungary;xx. Carlsberg Laboratory, Gamle Carlsbergvej 10, DK2500 Copenhagen, Denmark |
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Abstract: | The Zn(II) site of the dimeric Cu(II),Zn(II)-superoxide dismutase from Saccharomyces cerevisiae has been examined by means of perturbed angular correlation of gamma rays (PAC) on the Cu(II),Cd(II)- and Cu(I),Cd(II)-superoxide dismutase. The PAC spectrum for the Cu(II),Cd(II) enzyme reveals two different, pH independent, coordination geometries for the Cd site. Removal of Cu(II) does not affect the PAC spectrum, which suggests that Cu(II) and Cd(II) do not share a common histidine side chain as ligand. The results are consistent with either an equilibrium between two coordination geometries for Cd(II) in each subunit or a difference in the structure of the Cd(II) site in the two subunits. In contrast, in the reduced enzyme only one structure is present, identical for the two subunits. |
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Keywords: | TM tunicamycin KM kanamycin FCS fetal calf serum PI propidium iodide TCA trichloroacetic acid SDS sodium dodecyl sulfate |
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