These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y(Z) oxidation in photosystem II. Author: Sjödin M, Styring S, Akermark B, Sun L, Hammarström L. Journal: Philos Trans R Soc Lond B Biol Sci; 2002 Oct 29; 357(1426):1471-9; discussion 1478-9, 1511. PubMed ID: 12437887. 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.[Abstract] [Full Text] [Related] [New Search]