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  X-ray structure analysis of a membrane protein complex: Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis

Deisenhofer, J., Epp, O., Miki, K., Huber, R., & Michel, H. (1984). X-ray structure analysis of a membrane protein complex: Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. Journal of Molecular Biology (London), 180(2), 385-398. doi:10.1016/S0022-2836(84)80011-X.

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 Creators:
Deisenhofer, Johann1, Author
Epp, Otto1, Author
Miki, Kunio1, Author
Huber, Robert1, Author
Michel, Hartmut1, Author                 
Affiliations:
1Max Planck Institute of Biochemistry, Max Planck Society, ou_1565141              

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 Abstract: X-ray analysis of three-dimensional crystals of the photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis led to an electron density distribution at 3 Å resolution calculated with phases from multiple isomorphous replacement. The protein subunits of the complex were identified. An atomic model of the prosthetic groups of the reaction center complex (4 bacteriochlorophyll b, 2 bacteriopheophytin b, 1 non-heme iron, 1 menaquinone, 4 heme groups) was built. The arrangement of the ring systems of the bacteriochlorophyll b and bacteriopheophytin b molecules shows a local 2-fold rotation symmetry; two bacteriochlorophyll b form a closely associated, non-covalently linked dimer (“special pair”). A different local 2-fold symmetry axis is observed for the heme groups of the cytochrome part.

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Language(s): eng - English
 Dates: 1984-07-301984-07-0219842005-05-051984-12-05
 Publication Status: Issued
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0022-2836(84)80011-X
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 180 (2) Sequence Number: - Start / End Page: 385 - 398 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042