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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)

Abstract

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
Volume357
Issue number1426
DOIs
Publication statusPublished - 2002 Oct 29
Externally publishedYes

Keywords

  • 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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