. 2002 Oct 29;357(1426):1471-9; discussion 1478-9, 1511.
doi: 10.1098/rstb.2002.1142.
The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y(Z) oxidation in photosystem II
Affiliations
- PMID: 12437887
- PMCID: PMC1693043
- DOI: 10.1098/rstb.2002.1142
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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
Philos Trans R Soc Lond B Biol Sci.
.
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.
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