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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, E-ISSN 1471-2970, Vol. 357, no 1426, p. 1471-1478Article in journal (Refereed) Published
Abstract [en]

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, p. 1471-1478
Keyword [en]
photosystem II, proton-coupled electron transfer, tyrosine, ruthenium, photochemistry, oxygen, water, photosynthesis, chemistry
Identifiers
URN: urn:nbn:se:kth:diva-22029ISI: 000179103400029OAI: oai:DiVA.org:kth-22029DiVA, id: diva2:340727
Note
QC 20100525Available from: 2010-08-10 Created: 2010-08-10 Last updated: 2017-12-12Bibliographically approved

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