We have also completed the first characterization of the active site of NiSOD from Streptomyces seoulensis. This study reveals that Ni site is bound to thiolate donors, like other Ni redox enzymes but unlike any previously characterized SOD. Examination of oxidized and reduced samples reveal a coordination number change (5 -> 4) and a shift in the edge energy appropriate for a one-electron process. There is also evidence that the active site consists of two Ni centers, one of which is not redox active in analogy with the CuZnSOD, and therefore must be composed of two subunits in the tetrameric enzyme.
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