The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y-z oxidation in photosystem II
(2002) In Philosophical Transactions of the Royal Society B: Biological Sciences 357(1426). p.1471-1478- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/324146
- author
- Sjodin, M ; Styring, Stenbjörn LU ; Akermark, B and Sun, LC
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- tyrosine, photosystem II, proton-coupled electron transfer, photochemistry, ruthenium
- in
- Philosophical Transactions of the Royal Society B: Biological Sciences
- volume
- 357
- issue
- 1426
- pages
- 1471 - 1478
- publisher
- Royal Society Publishing
- external identifiers
-
- pmid:12437887
- wos:000179103400029
- scopus:0041405870
- pmid:12437887
- ISSN
- 1471-2970
- DOI
- 10.1098/rstb.2002.1142
- language
- English
- LU publication?
- yes
- id
- 5808775f-46d0-4945-ba27-368f8c26ba4c (old id 324146)
- date added to LUP
- 2016-04-01 17:01:24
- date last changed
- 2022-01-28 23:50:10
@article{5808775f-46d0-4945-ba27-368f8c26ba4c, 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.}}, author = {{Sjodin, M and Styring, Stenbjörn and Akermark, B and Sun, LC}}, issn = {{1471-2970}}, keywords = {{tyrosine; photosystem II; proton-coupled electron transfer; photochemistry; ruthenium}}, language = {{eng}}, number = {{1426}}, pages = {{1471--1478}}, publisher = {{Royal Society Publishing}}, series = {{Philosophical Transactions of the Royal Society B: Biological Sciences}}, title = {{The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y-z oxidation in photosystem II}}, url = {{http://dx.doi.org/10.1098/rstb.2002.1142}}, doi = {{10.1098/rstb.2002.1142}}, volume = {{357}}, year = {{2002}}, }