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 language | English |
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Pages (from-to) | 1471-1479 |
Number of pages | 9 |
Journal | Philosophical Transactions of the Royal Society B: Biological Sciences |
Volume | 357 |
Issue number | 1426 |
DOIs | |
Publication status | Published - 2002 Oct 29 |
Externally published | Yes |
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)