The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with YZ oxidation in photosystem II

Martin Sjödin, Stenbjörn Styring, Björn Åkermark, Licheng Sun, Leif Hammarström, A. Melis, C. Dismukes, P. L. Dutton, M. Aukauloo, R. D. Britt, M. Iwaki

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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 P680) 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 made and studied the proton-coupled tyrosine oxidation in a model system and been able to draw mechanistic conclusions that we use to interpret the analogous reactions in PSII.

Original languageEnglish
Pages (from-to)1471-1479
Number of pages9
JournalPhilosophical Transactions of the Royal Society B: Biological Sciences
Issue number1426
Publication statusPublished - Oct 29 2002



  • Photochemistry
  • Photosystem II
  • Proton-coupled electron transfer
  • Ruthenium
  • Tyrosine

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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