Abstract
Low-temperature (77 K) illumination of manganese-depleted Synechocystis PCC 6803 photosystem II core complexes caused the reversible photooxidation of a carotenoid, forming a carotenoid cation radical with an absorbance maximum at 984 nm. Resonance FT-Raman spectra obtained with 1064 nm excitation gave a spectrum characteristic of carotenoid cation radicals in solution. This is the first example of a resonance Raman spectrum of a carotenoid cation radical in a protein. The carotenoid photooxidation requires prior chemical oxidation of cytochrome b559 which implicates the carotenoid in the secondary electron-transfer pathway of photosystem II that may play a role in photoprotection. The possible nature of the pathway and the structure of the carotenoid cation radical are discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 6403-6406 |
| Number of pages | 4 |
| Journal | Journal of Physical Chemistry B |
| Volume | 103 |
| Issue number | 31 |
| Publication status | Published - Aug 5 1999 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
Cite this
Low-Temperature Optical and Resonance Raman Spectra of a Carotenoid Cation Radical in Photosystem II. / Vrettos, John S.; Stewart, David H.; De Paula, Julio C.; Brudvig, Gary W.
In: Journal of Physical Chemistry B, Vol. 103, No. 31, 05.08.1999, p. 6403-6406.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Low-Temperature Optical and Resonance Raman Spectra of a Carotenoid Cation Radical in Photosystem II
AU - Vrettos, John S.
AU - Stewart, David H.
AU - De Paula, Julio C.
AU - Brudvig, Gary W
PY - 1999/8/5
Y1 - 1999/8/5
N2 - Low-temperature (77 K) illumination of manganese-depleted Synechocystis PCC 6803 photosystem II core complexes caused the reversible photooxidation of a carotenoid, forming a carotenoid cation radical with an absorbance maximum at 984 nm. Resonance FT-Raman spectra obtained with 1064 nm excitation gave a spectrum characteristic of carotenoid cation radicals in solution. This is the first example of a resonance Raman spectrum of a carotenoid cation radical in a protein. The carotenoid photooxidation requires prior chemical oxidation of cytochrome b559 which implicates the carotenoid in the secondary electron-transfer pathway of photosystem II that may play a role in photoprotection. The possible nature of the pathway and the structure of the carotenoid cation radical are discussed.
AB - Low-temperature (77 K) illumination of manganese-depleted Synechocystis PCC 6803 photosystem II core complexes caused the reversible photooxidation of a carotenoid, forming a carotenoid cation radical with an absorbance maximum at 984 nm. Resonance FT-Raman spectra obtained with 1064 nm excitation gave a spectrum characteristic of carotenoid cation radicals in solution. This is the first example of a resonance Raman spectrum of a carotenoid cation radical in a protein. The carotenoid photooxidation requires prior chemical oxidation of cytochrome b559 which implicates the carotenoid in the secondary electron-transfer pathway of photosystem II that may play a role in photoprotection. The possible nature of the pathway and the structure of the carotenoid cation radical are discussed.
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M3 - Article
VL - 103
SP - 6403
EP - 6406
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
SN - 1520-6106
IS - 31
ER -