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 P680) 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.
| Original language | English |
|---|---|
| Pages (from-to) | 1471-1479 |
| Number of pages | 9 |
| Journal | Philosophical Transactions of the Royal Society B: Biological Sciences |
| Volume | 357 |
| Issue number | 1426 |
| DOIs | |
| Publication status | Published - 2002 Oct 29 |
| Externally published | Yes |
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Keywords
- Photochemistry
- Photosystem II
- Proton-coupled electron transfer
- Ruthenium
- Tyrosine
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)
Cite this
The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with YZ oxidation in photosystem II. / Sjödin, Martin; Styring, Stenbjörn; Åkermark, Björn; Sun, Licheng; Hammarström, Leif; Melis, A.; Dismukes, C.; Dutton, P. L.; Aukauloo, M.; Britt, R. D.; Iwaki, M.
In: Philosophical Transactions of the Royal Society B: Biological Sciences, Vol. 357, No. 1426, 29.10.2002, p. 1471-1479.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with YZ oxidation in photosystem II
AU - Sjödin, Martin
AU - Styring, Stenbjörn
AU - Åkermark, Björn
AU - Sun, Licheng
AU - Hammarström, Leif
AU - Melis, A.
AU - Dismukes, C.
AU - Dutton, P. L.
AU - Aukauloo, M.
AU - Britt, R. D.
AU - Iwaki, M.
PY - 2002/10/29
Y1 - 2002/10/29
N2 - 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 P680) 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.
AB - 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 P680) 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.
KW - Photochemistry
KW - Photosystem II
KW - Proton-coupled electron transfer
KW - Ruthenium
KW - Tyrosine
UR - http://www.scopus.com/inward/record.url?scp=0041405870&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0041405870&partnerID=8YFLogxK
U2 - 10.1098/rstb.2002.1142
DO - 10.1098/rstb.2002.1142
M3 - Article
VL - 357
SP - 1471
EP - 1479
JO - Philosophical Transactions of the Royal Society B: Biological Sciences
JF - Philosophical Transactions of the Royal Society B: Biological Sciences
SN - 0962-8436
IS - 1426
ER -