Mixed exciton–charge-transfer states in photosystem II: Stark spectroscopy on site–directed mutants

E. Romero Mesa; B.A. Diner; P.J. Nixon; W.J. Coleman; J.P. Dekker; R. van Grondelle

doi:10.1016/j.bpj.2012.06.026

Mixed exciton–charge-transfer states in photosystem II: Stark spectroscopy on site–directed mutants

E. Romero Mesa, B.A. Diner, P.J. Nixon, W.J. Coleman, J.P. Dekker, R. van Grondelle

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

We investigated the electronic structure of the photosystem II reaction center (PSII RC) in relation to the light-induced charge separation process using Stark spectroscopy on a series of site-directed PSII RC mutants from the cyanobacterium Synechocystis sp. PCC 6803. The site-directed mutations modify the protein environment of the cofactors involved in charge separation (P

Original language	English
Pages (from-to)	185-194
Journal	Biophysical Journal
Volume	103
Issue number	2
DOIs	https://doi.org/10.1016/j.bpj.2012.06.026
Publication status	Published - 2012

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Romero Mesa, E., Diner, B. A., Nixon, P. J., Coleman, W. J., Dekker, J. P., & van Grondelle, R. (2012). Mixed exciton–charge-transfer states in photosystem II: Stark spectroscopy on site–directed mutants. Biophysical Journal, 103(2), 185-194. https://doi.org/10.1016/j.bpj.2012.06.026

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abstract = "We investigated the electronic structure of the photosystem II reaction center (PSII RC) in relation to the light-induced charge separation process using Stark spectroscopy on a series of site-directed PSII RC mutants from the cyanobacterium Synechocystis sp. PCC 6803. The site-directed mutations modify the protein environment of the cofactors involved in charge separation (P",

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AU - van Grondelle, R.

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AB - We investigated the electronic structure of the photosystem II reaction center (PSII RC) in relation to the light-induced charge separation process using Stark spectroscopy on a series of site-directed PSII RC mutants from the cyanobacterium Synechocystis sp. PCC 6803. The site-directed mutations modify the protein environment of the cofactors involved in charge separation (P

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10.1016/j.bpj.2012.06.026

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