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Three-dimensional structure of photosystem-II reaction centre at 8Å resolution

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Rhee,  Kyong-Hi
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
EMBL, Structural Biology Programme and Biocomputing Unit, Meyerhofstrasse 1, D-69117, Heidelberg, Germany;

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Kühlbrandt,  Werner
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Rhee, K.-H., Morris, E. P., Barber, J., & Kühlbrandt, W. (1998). Three-dimensional structure of photosystem-II reaction centre at 8Å resolution. Nature, 396(6708), 283-286. doi:10.1038/24421.


Cite as: http://hdl.handle.net/21.11116/0000-0007-A236-5
Abstract
Photosystem II is a multisubunit enzyme complex involved in plant photosynthesis. It uses solar energy to catalyse the breakdown of water to reducing equivalents and molecular oxygen1. Native photosystem II comprises more than 25 different subunits, and has a relative molecular mass of more than 600K. Here we report the three-dimensional structure of a photosystem II subcomplex, containing the proteins D1, D2, CP47 and cytochrome b -559, determined by electron crystallography. This CP47 reaction centre, which has a relative molecular mass of 160K, can perform light-mediated energy and electron-transfer reactions but is unable to oxidize water2. The complex contains 23 transmembrane α-helices, of which 16 have been assigned to the D1, D2 and CP47 proteins. The arrangement of these helices is remarkably similar to that of the helices in the reaction centres of purple bacteria and of plant photosystem I, indicating a common evolutionary origin for these assemblies. The map suggests that redox cofactors in the D1–D2 complex are located in positions analogous to those in the bacterial reaction centre, but the distance between the chlorophylls corresponding to the bacterial ‘special pair’ is significantly larger.