Abstract
This review describes the progress in our understanding of the structure of the Mn complex in Photosystem II over the last two decades. Emphasis is on the research from our laboratory, especially the results from X-ray absorption spectroscopy, low temperature electron paramagnetic resonance and electron spin echo envelope modulation studies. The importance of the interplay between electron paramagnetic resonance studies and X-ray absorption studies, which has led to a description of the oxidation states of manganese as the enzyme cycles through the Kok cycle, is described. Finally, the path, by which our group has utilized these two important methods to arrive at a working structural model for the manganese complex that catalyzes the oxidation of water to dioxygen in higher plants and cyanobacteria, is explained.
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