Abstract
Orientations and relative positions of paramagnetic intermediates in protein complexes of Photosystem (PS) II can be studied by electron paramagnetic resonance (EPR) spectroscopy. The EPR spectroscopic approaches and results on components of the electron transfer chain in PS II are presented. Where possible the data from EPR spectroscopy are compared to structural data from X-ray analysis. This comparison shows that the EPR-derived orientations and distances between the redox partners in PS II are in general corroborated by the recent X-ray crystallographic models. Furthermore, specific experiments that complement information available from crystallography are discussed.
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