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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

Sjodin, M; Styring, Stenbjörn LU ; Akermark, B and Sun, LC (2002) In Royal Society of London. Philosophical Transactions 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.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
tyrosine, photosystem II, proton-coupled electron transfer, photochemistry, ruthenium
in
Royal Society of London. Philosophical Transactions B. Biological Sciences
volume
357
issue
1426
pages
1471 - 1478
publisher
Royal Society
external identifiers
  • pmid:12437887
  • wos:000179103400029
  • scopus:0041405870
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
2007-11-14 12:30:46
date last changed
2017-08-06 04:40:40
@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},
  keyword      = {tyrosine,photosystem II,proton-coupled electron transfer,photochemistry,ruthenium},
  language     = {eng},
  number       = {1426},
  pages        = {1471--1478},
  publisher    = {Royal Society},
  series       = {Royal Society of London. Philosophical Transactions 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},
  volume       = {357},
  year         = {2002},
}