Abstract
Mn plays a key role in a variety of redox proteins, including superoxide dismutase (mononuclear Mn site), catalase (dinuclear Mn site) and the photosynthetic oxygen evolving complex (tetranuclear Mn site). Recent work on the structural, kinetic, and spectroscopic characterization of the Mn sites in the catalase and in Mn and Fe superoxide dismutase will be described. For Mn catalase, a combination of activity measurements, EPR and x-ray absorption spectroscopy [ 1,2] has lead to the kinetic model shown in Fig. 1,
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