The mechanism for proton–coupled electron transfer from tyrosine in a model complex and comparisons with Y Z oxidation in photosystem II
Open Access
- 29 October 2002
- journal article
- Published by The Royal Society in Philosophical Transactions Of The Royal Society B-Biological Sciences
- Vol. 357 (1426) , 1471-1479
- https://doi.org/10.1098/rstb.2002.1142
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 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.Keywords
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