The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y-z oxidation in photosystem II
2002 (English)In: Philosophical Transactions of the Royal Society of London. Biological Sciences, ISSN 0962-8436, Vol. 357, no 1426, 1471-1478 p.Article in journal (Refereed) Published
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 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.
Place, publisher, year, edition, pages
2002. Vol. 357, no 1426, 1471-1478 p.
photosystem II, proton-coupled electron transfer, tyrosine, ruthenium, photochemistry, oxygen, water, photosynthesis, chemistry
IdentifiersURN: urn:nbn:se:kth:diva-22029ISI: 000179103400029OAI: oai:DiVA.org:kth-22029DiVA: diva2:340727
QC 201005252010-08-102010-08-10Bibliographically approved