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  Lipids in photosystem II: Interactions with protein and cofactors

Loll, B., Kern, J., Saenger, W., Zouni, A., & Biesiadka, J. (2007). Lipids in photosystem II: Interactions with protein and cofactors. Biochimica et Biophysica Acta, Bioenergetics, 1767(6), 509-519. doi:10.1016/j.bbabio.2006.12.009.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-AB8C-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-AB8D-B
Genre: Journal Article
Alternative Title : Lipids in photosystem II: Interactions with protein and cofactors

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 Creators:
Loll, Bernhard1, Author              
Kern, Jan, Author
Saenger, Wolfram, Author
Zouni, Athina, Author
Biesiadka, Jacek, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Photosystem II; Structure; Lipids; Dimerization; Thylakoid membrane; Plastoquinone diffusion
 Abstract: Photosystem II (PSII) is a homodimeric protein–cofactor complex embedded in the thylakoid membrane that catalyses light-driven charge separation accompanied by the oxidation of water during oxygenic photosynthesis. Biochemical analysis of the lipid content of PSII indicates a number of integral lipids, their composition being similar to the average lipid composition of the thylakoid membrane. The crystal structure of PSII at 3.0 Å resolution allowed for the first time the assignment of 14 integral lipids within the protein scaffold, all of them being located at the interface of different protein subunits. The reaction centre subunits D1 and D2 are encircled by a belt of 11 lipids providing a flexible environment for the exchange of D1. Three lipids are located in the dimerization interface and mediate interactions between the PSII monomers. Several lipids are located close to the binding pocket of the mobile plastoquinone QB, forming part of a postulated diffusion pathway for plastoquinone. Furthermore two lipids were found, each ligating one antenna chlorophyll a. A detailed analysis of lipid–protein and lipid–cofactor interactions allows to derive some general principles of lipid binding pockets in PSII and to suggest possible functional properties of the various identified lipid molecules.

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Language(s): eng - English
 Dates: 2006-12-142006-10-202006-12-192007-01-042007-06-01
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Biochimica et Biophysica Acta, Bioenergetics
  Abbreviation : Biochim. Biophys. Acta, Bioenerg.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: 11 Volume / Issue: 1767 (6) Sequence Number: - Start / End Page: 509 - 519 Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6