An iron-containing superoxide dismutase from Anacystis nidulans.
J Biochem, 1979/6;85(6):1397-404.
Cséke C, Horváth LL, Simon P, Borbély G, Keszthelyi L, Farkas GL
PMID: 222743
Impact factor: 3.241
Abstract
Superoxide dismutase (SOD) was isolated and purified from Anacystis nidulans to near electrophoretic homogeneity. The enzyme has a molecular weight of 37,500, as determined by gel filtration and SDS-gel electrophoresis. The enzyme molecule consists of two subunits of identical molecular weight. Proton-induced X-ray elemental analysis (PIXE) showed that the SOD of A. nidulans is an iron-containing enzyme; the Fe:enzyme mol ratio was found to be 1. The EPR spectra indicated that the active center contains high-spin ferric ion. Based on quantitative EPR data, we conclude that eseentially all iron ions were detected in the EPR experiments and were present in the Fe3+ active center. Effective g'-values were calculated from computer-simulated spectra and analysis of the g'-value anisotropy of the +/-3/2 Kramers doublet made the calculation of crystal field parameters possible. The symmetry of the Fe3+ ion in the SOD molecule was found to be close to rhombic (E/D=0.240).
MeSH terms
Binding Sites; Cyanobacteria; Electron Spin Resonance Spectroscopy; Iron; Macromolecular Substances; Molecular Conformation; Molecular Weight; Superoxide Dismutase
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