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  Function of two β−carotenes near the D1 and D2 proteins in photosystem II dimers

Ishikita, H., Loll, B., Biesiadka, J., Kern, J., Irrgang, K., Zouni, A., et al. (2007). Function of two β−carotenes near the D1 and D2 proteins in photosystem II dimers. Biochimica et Biophysica Acta-Bioenergetics, 1767(1), 79-87. doi:10.1016/j.bbabio.2006.10.006.

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Genre: Journal Article
Alternative Title : Function of two β−carotenes near the D1 and D2 proteins in photosystem II dimers

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BBA_1767_2007_79.pdf (Any fulltext), 755KB
 
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 Creators:
Ishikita, H., Author
Loll, Bernhard1, Author           
Biesiadka, Jacek, Author
Kern, Jana2, Author           
Irrgang, Klaus−Dieter, Author
Zouni, Athina, Author
Saenger, Wolfram, Author
Knapp, E. W., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              

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Free keywords: Photosystem II; Chlorophyll; β−carotene; Photoprotection; Electron transfer; Redox potential
 Abstract: The antenna proteins in photosystem II (PSII) not only promote energy transfer to the photosynthetic reaction center (RC) but provide also an efficient cation sink to re-reduce chlorophyll a if the electron transfer (ET) from the Mn-cluster is inhibited. Using the newest PSII dimer crystal structure (3.0 Å resolution), in which 11 β-carotene molecules (Car) and 14 lipids are visible in the PSII monomer, we calculated the redox potentials (Em) of one-electron oxidation for all Car (Em(Car)) by solving the Poisson–Boltzmann equation. In each PSII monomer, the D1 protein harbors a previously unlocated Car (CarD1) in van der Waals contact with the chlorin ring of ChlZ(D1). Each CarD1 in the PSII dimer complex is located in the interface between the D1 and CP47 subunits, together with another four Car of the other PSII monomer and several lipid molecules. The proximity of Car bridging between CarD1 and plastoquinone/QA may imply a direct charge recombination of Car+QA−. The calculated Em(CarD1) and Em(ChlZ(D1)) are, respectively, 83 and 126 mV higher than Em(CarD2) and Em(ChlZ(D2)), which could explain why CarD2+ and ChlZ(D2)+ are observed rather than the corresponding CarD1+ and ChlZ(D1)+.

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Language(s): eng - English
 Dates: 2006-10-112006-08-102006-10-122006-10-182007-01-01
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Biochimica et Biophysica Acta-Bioenergetics
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1767 (1) Sequence Number: - Start / End Page: 79 - 87 Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6