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Fiege R, Zweygart W, Bittl R, et al. EPR and ENDOR studies of the water oxidizing complex of Photosystem II. Photosynth Res. 1996;48(1):227-37doi: 10.1007/BF00041013.
Fiege, R., Zweygart, W., Bittl, R., Adir, N., Renger, G., & Lubitz, W. (1996). EPR and ENDOR studies of the water oxidizing complex of Photosystem II. Photosynthesis research, 48(1), 227-37. https://doi.org/10.1007/BF00041013
Fiege, R, et al. "EPR and ENDOR studies of the water oxidizing complex of Photosystem II." Photosynthesis research vol. 48,1 (1996): 227-37. doi: https://doi.org/10.1007/BF00041013
Fiege R, Zweygart W, Bittl R, Adir N, Renger G, Lubitz W. EPR and ENDOR studies of the water oxidizing complex of Photosystem II. Photosynth Res. 1996 May;48(1):227-37. doi: 10.1007/BF00041013. PMID: 24271303.
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Photosynth Res. 1996 May;48(1):227-37. doi: 10.1007/BF00041013.

EPR and ENDOR studies of the water oxidizing complex of Photosystem II.

Photosynthesis research

R Fiege, W Zweygart, R Bittl, N Adir, G Renger, W Lubitz

Affiliations

  1. Max Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität Berlin, Str. des 17. Juni 135, D-10623, Berlin, Germany.

PMID: 24271303 DOI: 10.1007/BF00041013

Abstract

A comparative study of X-band EPR and ENDOR of the S2 state of photosystem II membrane fragments and core complexes in the frozen state is presented. The S2 state was generated either by continuous illumination at T=200 K or by a single turn-over light flash at T=273 K yielding entirely the same S2 state EPR signals at 10 K. In membrane fragments and core complex preparations both the multiline and the g=4.1 signals were detected with comparable relative intensity. The absence of the 17 and 23 kDa proteins in the core complex preparation has no effect on the appearance of the EPR signals. (1)H-ENDOR experiments performed at two different field positions of the S2 state multiline signal of core complexes permitted the resolution of four hyperfine (hf) splittings. The hf coupling constants obtained are 4.0, 2.3, 1.1 and 0.6 MHz, in good agreement with results that were previously reported (Tang et al. (1993) J Am Chem Soc 115: 2382-2389). The intensities of all four line pairs belonging to these hf couplings are diminished in D2O. A novel model is presented and on the basis of the two largest hfc's distances between the manganese ions and the exchangeable protons are deduced. The interpretation of the ENDOR data indicates that these hf couplings might arise from water which is directly ligated to the manganese of the water oxidizing complex in redox state S2.

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