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  Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II

Loll, B., Kern, J., Saenger, W., Zouni, A., & Biesiadka, J. (2005). Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II. Nature, 438(7070), 1040-1044. doi:10.1038/nature04224.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-5042-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-5043-8
Genre: Journal Article

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Nature_438_2005_1040.pdf (Any fulltext), 528KB
 
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 Creators:
Loll, Bernhard1, Author              
Kern, Jana2, Author              
Saenger, Wolfram, Author
Zouni, Athina, Author
Biesiadka, Jacek, Author
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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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 Abstract: Oxygenic photosynthesis in plants, algae and cyanobacteria is initiated at photosystem II, a homodimeric multisubunit protein-cofactor complex embedded in the thylakoid membrane. Photosystem II captures sunlight and powers the unique photo-induced oxidation of water to atmospheric oxygen. Crystallographic investigations of cyanobacterial photosystem II have provided several medium-resolution structures (3.8 to 3.2 A) that explain the general arrangement of the protein matrix and cofactors, but do not give a full picture of the complex. Here we describe the most complete cyanobacterial photosystem II structure obtained so far, showing locations of and interactions between 20 protein subunits and 77 cofactors per monomer. Assignment of 11 beta-carotenes yields insights into electron and energy transfer and photo-protection mechanisms in the reaction centre and antenna subunits. The high number of 14 integrally bound lipids reflects the structural and functional importance of these molecules for flexibility within and assembly of photosystem II. A lipophilic pathway is proposed for the diffusion of secondary plastoquinone that transfers redox equivalents from photosystem II to the photosynthetic chain. The structure provides information about the Mn4Ca cluster, where oxidation of water takes place. Our study uncovers near-atomic details necessary to understand the processes that convert light to chemical energy.

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Language(s): eng - English
 Dates: 2005-07-012005-09-132005-12-14
 Publication Status: Published in print
 Pages: 5
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 Rev. Type: Peer
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 438 (7070) Sequence Number: - Start / End Page: 1040 - 1044 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238