The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y(Z) oxidation in photosystem II.

@article{Sjdin2002TheMF,
  title={The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y(Z) oxidation in photosystem II.},
  author={Martin Sj{\"o}din and Stenbj{\"o}rn Styring and Bj{\"o}rn {\AA}kermark and Licheng Sun and Leif Hammarstr{\"o}m},
  journal={Philosophical transactions of the Royal Society of London. Series B, Biological sciences},
  year={2002},
  volume={357 1426},
  pages={1471-9; discussion 1478-9, 1511}
}
In the water-oxidizing reactions of photosystem II (PSII), a tyrosine residue plays a key part as an intermediate electron-transfer reactant between the primary donor chlorophylls (the pigment P(680)) and the water-oxidizing Mn cluster. The tyrosine is deprotonated upon oxidation, and the coupling between the proton reaction and electron transfer is of great mechanistic importance for the understanding of the water-oxidation mechanism. Within a programme on artificial photosynthesis, we have… CONTINUE READING

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