Abstract
When the primary electron-donation pathway from the water-oxidation complex in photosystem II (PS II) is inhibited, chlorophyll (ChlZ and ChlD), β-carotene (Car) and cytochrome b559 are alternate electron donors that are believed to function in a photoprotection mechanism. Previous studies have demonstrated that high-frequency EPR spectroscopy (at 130 GHz), together with deuteration of PS II, yields resolved Car+ and Chl+ EPR signals (Lakshmi et al. J. Phys. Chem. B 2000, 104, 10 445-10 448). The present study describes the use of pulsed high-frequency EPR spectroscopy to measure the location of the carotenoid and chlorophyll radicals relative to other paramagnetic cofactors in Synechococcus lividus PS II. The spin-lattice relaxation rates of the Car+ and Chl+ radicals are measured in manganese-depleted and manganese-depleted, cyanide-treated PS II; in these samples, the non-heme Fe(II) is high-spin (S = 2) and low-spin (S = 0), respectively. The Car+ and Chl+ radicals exhibit dipolar-enhanced relaxation rates in the presence of high-spin (S = 2) Fe(II) that are eliminated when the Fe(II) is low-spin (S = 0). The relaxation enhancements of the Car+ and Chl+ by the non-heme Fe(II) are smaller than the relaxation enhancement of TyrD· and P865 + by the non-heme Fe(II) in PS II and in the reaction center from Rhodobacter sphaeroides, respectively, indicating that the Car+-Fe(II) and Chl+-Fe(II) distances are greater than the known TyrD·-Fe(II) and P865 +-Fe(II) distances. The Car+ radical exhibits a greater relaxation enhancement by Fe(II) than the Chl+ radical, consistent with Car being an earlier electron donor to P680 + than Chl. On the basis of the distance estimates obtained in the present study and by analogy to carotenoid-binding sites in other pigment-protein complexes, possible binding sites are discussed for the Car cofactors in PS II. The relative location of Car+ and Chl+ radicals determined in this study provides valuable insight into the sequence of electron transfers in the alternate electron-donation pathways of PS II.
| Original language | English |
|---|---|
| Pages (from-to) | 5005-5014 |
| Number of pages | 10 |
| Journal | Journal of the American Chemical Society |
| Volume | 125 |
| Issue number | 17 |
| Publication status | Published - Apr 30 2003 |
Fingerprint
ASJC Scopus subject areas
- Chemistry(all)
Cite this
Pulsed high-frequency EPR study on the location of carotenoid and chlorophyll cation radicals in photosystem II. / Lakshmi, K. V.; Poluektov, Oleg G.; Reifler, Michael J.; Wagner, Arlene M.; Thurnauer, Marion C.; Brudvig, Gary W.
In: Journal of the American Chemical Society, Vol. 125, No. 17, 30.04.2003, p. 5005-5014.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Pulsed high-frequency EPR study on the location of carotenoid and chlorophyll cation radicals in photosystem II
AU - Lakshmi, K. V.
AU - Poluektov, Oleg G.
AU - Reifler, Michael J.
AU - Wagner, Arlene M.
AU - Thurnauer, Marion C.
AU - Brudvig, Gary W.
PY - 2003/4/30
Y1 - 2003/4/30
N2 - When the primary electron-donation pathway from the water-oxidation complex in photosystem II (PS II) is inhibited, chlorophyll (ChlZ and ChlD), β-carotene (Car) and cytochrome b559 are alternate electron donors that are believed to function in a photoprotection mechanism. Previous studies have demonstrated that high-frequency EPR spectroscopy (at 130 GHz), together with deuteration of PS II, yields resolved Car+ and Chl+ EPR signals (Lakshmi et al. J. Phys. Chem. B 2000, 104, 10 445-10 448). The present study describes the use of pulsed high-frequency EPR spectroscopy to measure the location of the carotenoid and chlorophyll radicals relative to other paramagnetic cofactors in Synechococcus lividus PS II. The spin-lattice relaxation rates of the Car+ and Chl+ radicals are measured in manganese-depleted and manganese-depleted, cyanide-treated PS II; in these samples, the non-heme Fe(II) is high-spin (S = 2) and low-spin (S = 0), respectively. The Car+ and Chl+ radicals exhibit dipolar-enhanced relaxation rates in the presence of high-spin (S = 2) Fe(II) that are eliminated when the Fe(II) is low-spin (S = 0). The relaxation enhancements of the Car+ and Chl+ by the non-heme Fe(II) are smaller than the relaxation enhancement of TyrD· and P865 + by the non-heme Fe(II) in PS II and in the reaction center from Rhodobacter sphaeroides, respectively, indicating that the Car+-Fe(II) and Chl+-Fe(II) distances are greater than the known TyrD·-Fe(II) and P865 +-Fe(II) distances. The Car+ radical exhibits a greater relaxation enhancement by Fe(II) than the Chl+ radical, consistent with Car being an earlier electron donor to P680 + than Chl. On the basis of the distance estimates obtained in the present study and by analogy to carotenoid-binding sites in other pigment-protein complexes, possible binding sites are discussed for the Car cofactors in PS II. The relative location of Car+ and Chl+ radicals determined in this study provides valuable insight into the sequence of electron transfers in the alternate electron-donation pathways of PS II.
AB - When the primary electron-donation pathway from the water-oxidation complex in photosystem II (PS II) is inhibited, chlorophyll (ChlZ and ChlD), β-carotene (Car) and cytochrome b559 are alternate electron donors that are believed to function in a photoprotection mechanism. Previous studies have demonstrated that high-frequency EPR spectroscopy (at 130 GHz), together with deuteration of PS II, yields resolved Car+ and Chl+ EPR signals (Lakshmi et al. J. Phys. Chem. B 2000, 104, 10 445-10 448). The present study describes the use of pulsed high-frequency EPR spectroscopy to measure the location of the carotenoid and chlorophyll radicals relative to other paramagnetic cofactors in Synechococcus lividus PS II. The spin-lattice relaxation rates of the Car+ and Chl+ radicals are measured in manganese-depleted and manganese-depleted, cyanide-treated PS II; in these samples, the non-heme Fe(II) is high-spin (S = 2) and low-spin (S = 0), respectively. The Car+ and Chl+ radicals exhibit dipolar-enhanced relaxation rates in the presence of high-spin (S = 2) Fe(II) that are eliminated when the Fe(II) is low-spin (S = 0). The relaxation enhancements of the Car+ and Chl+ by the non-heme Fe(II) are smaller than the relaxation enhancement of TyrD· and P865 + by the non-heme Fe(II) in PS II and in the reaction center from Rhodobacter sphaeroides, respectively, indicating that the Car+-Fe(II) and Chl+-Fe(II) distances are greater than the known TyrD·-Fe(II) and P865 +-Fe(II) distances. The Car+ radical exhibits a greater relaxation enhancement by Fe(II) than the Chl+ radical, consistent with Car being an earlier electron donor to P680 + than Chl. On the basis of the distance estimates obtained in the present study and by analogy to carotenoid-binding sites in other pigment-protein complexes, possible binding sites are discussed for the Car cofactors in PS II. The relative location of Car+ and Chl+ radicals determined in this study provides valuable insight into the sequence of electron transfers in the alternate electron-donation pathways of PS II.
UR - http://www.scopus.com/inward/record.url?scp=0242584836&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0242584836&partnerID=8YFLogxK
M3 - Article
C2 - 12708850
AN - SCOPUS:0242584836
VL - 125
SP - 5005
EP - 5014
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 17
ER -