Identifying the lowest electronic states of the chlorophylls in the CP47 core antenna protein of photosystem II

F.L. de Weerd, M.A. Palacios, E. Andrizhiyevskaya, J.P. Dekker, R. van Grondelle

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

CP47 is a pigment-protein complex in the core of photosystem II that tranfers excitation energy to the reaction center. Here we report on a spectroscopic investigation of the isolated CP47 complex. By deconvoluting the 77 K absorption and linear dichroism, red-most states at 683 and 690 nm have been identified with oscillator strengths corresponding to ∼3 and ∼1 chlorophyll, respectively. Both states contribute to the 4 K emission, and the Stark spectrum shows that they have a large value for the difference polarizability between their ground and excited states. From site-selective polarized triplet-minus-singlet spectra, an excitonic origin for the 683 nm state was found. The red shift of the 690 nm state is most probably due to strong hydrogen bonding to a protein ligand, as follows from the position of the stretch frequency of the chlorophyll 13
Original languageEnglish
Pages (from-to)15224-15233
JournalBiochemistry
Volume41
Issue number51
DOIs
Publication statusPublished - 2002

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Photosystem II Protein Complex
Electronic states
Chlorophyll
Antennas
Excitation energy
Hydrogen Bonding
Excited states
Pigments
Ground state
Hydrogen bonds
Proteins
Ligands

Bibliographical note

Identifying the lowest electronic states of the chlorophylls in the CP47 core antenna protein of photosystem II

Cite this

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title = "Identifying the lowest electronic states of the chlorophylls in the CP47 core antenna protein of photosystem II",
abstract = "CP47 is a pigment-protein complex in the core of photosystem II that tranfers excitation energy to the reaction center. Here we report on a spectroscopic investigation of the isolated CP47 complex. By deconvoluting the 77 K absorption and linear dichroism, red-most states at 683 and 690 nm have been identified with oscillator strengths corresponding to ∼3 and ∼1 chlorophyll, respectively. Both states contribute to the 4 K emission, and the Stark spectrum shows that they have a large value for the difference polarizability between their ground and excited states. From site-selective polarized triplet-minus-singlet spectra, an excitonic origin for the 683 nm state was found. The red shift of the 690 nm state is most probably due to strong hydrogen bonding to a protein ligand, as follows from the position of the stretch frequency of the chlorophyll 13",
author = "{de Weerd}, F.L. and M.A. Palacios and E. Andrizhiyevskaya and J.P. Dekker and {van Grondelle}, R.",
note = "Identifying the lowest electronic states of the chlorophylls in the CP47 core antenna protein of photosystem II",
year = "2002",
doi = "10.1021/bi0261948",
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journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
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Identifying the lowest electronic states of the chlorophylls in the CP47 core antenna protein of photosystem II. / de Weerd, F.L.; Palacios, M.A.; Andrizhiyevskaya, E.; Dekker, J.P.; van Grondelle, R.

In: Biochemistry, Vol. 41, No. 51, 2002, p. 15224-15233.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Identifying the lowest electronic states of the chlorophylls in the CP47 core antenna protein of photosystem II

AU - de Weerd, F.L.

AU - Palacios, M.A.

AU - Andrizhiyevskaya, E.

AU - Dekker, J.P.

AU - van Grondelle, R.

N1 - Identifying the lowest electronic states of the chlorophylls in the CP47 core antenna protein of photosystem II

PY - 2002

Y1 - 2002

N2 - CP47 is a pigment-protein complex in the core of photosystem II that tranfers excitation energy to the reaction center. Here we report on a spectroscopic investigation of the isolated CP47 complex. By deconvoluting the 77 K absorption and linear dichroism, red-most states at 683 and 690 nm have been identified with oscillator strengths corresponding to ∼3 and ∼1 chlorophyll, respectively. Both states contribute to the 4 K emission, and the Stark spectrum shows that they have a large value for the difference polarizability between their ground and excited states. From site-selective polarized triplet-minus-singlet spectra, an excitonic origin for the 683 nm state was found. The red shift of the 690 nm state is most probably due to strong hydrogen bonding to a protein ligand, as follows from the position of the stretch frequency of the chlorophyll 13

AB - CP47 is a pigment-protein complex in the core of photosystem II that tranfers excitation energy to the reaction center. Here we report on a spectroscopic investigation of the isolated CP47 complex. By deconvoluting the 77 K absorption and linear dichroism, red-most states at 683 and 690 nm have been identified with oscillator strengths corresponding to ∼3 and ∼1 chlorophyll, respectively. Both states contribute to the 4 K emission, and the Stark spectrum shows that they have a large value for the difference polarizability between their ground and excited states. From site-selective polarized triplet-minus-singlet spectra, an excitonic origin for the 683 nm state was found. The red shift of the 690 nm state is most probably due to strong hydrogen bonding to a protein ligand, as follows from the position of the stretch frequency of the chlorophyll 13

U2 - 10.1021/bi0261948

DO - 10.1021/bi0261948

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SP - 15224

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JF - Biochemistry

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