title: Comparative studies of the S0 and S2 multiline electron paramagnetic resonance signals from the manganese cluster in Photosystem II.
abstract: Electron paramagnetic resonance (EPR) spectroscopy is one of the major techniques used to analyse the structure and function of the water oxidising complex (WOC) in Photosystem II. The discovery of an EPR signal from the S0 state has opened the way for new experiments, aiming to characterise the S0 state and elucidate the differences between the different S states. We present a review of the biochemical and biophysical characterisation of the S0 state multiline signal that has evolved since its discovery, and compare these results to previous and recent data from the S2 multiline signal. We also present some new data from the S2 state reached on the second turnover of the enzyme.
authors: Department of Biochemistry, Centre for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, S-221 00, Lund, Sweden.
authors: P
authors: P
authors: Geijer
authors: S
authors: S
authors: Peterson
authors: K A
authors: KA
authors: Ahrling
authors: Z
authors: Z
authors: Deák
authors: S
authors: S
authors: Styring
mesh_terms: D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D008345:Manganese / Q000737:chemistry*; D000432:Methanol; D008872:Microwaves; D009942:Organometallic Compounds / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D045332:Photosystem II Protein Complex; D013696:Temperature; D014867:Water / Q000737:chemistry
chemical_list: D009942:Organometallic Compounds; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D014867:Water; D008345:Manganese; D010100:Oxygen; D000432:Methanol