Two-dimensional structure of plant photosystem II at 8-Å resolution

Kyong-Hi Rhee, Ed P. Morris, Daniela Zheleva, Ben Hankamer, Werner Kühlbrandt () and James Barber
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Kyong-Hi Rhee: European Molecular Biology Laboratory
Ed P. Morris: Wolfson Laboratories, Imperial College of Science, Technology and Medicine
Daniela Zheleva: Wolfson Laboratories, Imperial College of Science, Technology and Medicine
Ben Hankamer: Wolfson Laboratories, Imperial College of Science, Technology and Medicine
Werner Kühlbrandt: European Molecular Biology Laboratory
James Barber: Wolfson Laboratories, Imperial College of Science, Technology and Medicine

Nature, 1997, vol. 389, issue 6650, 522-526

Abstract: Abstract The photosystem II complex, which is the most abundant membrane protein in chloroplasts, comprises the light-harvesting complex II and a reaction-centre core. The reaction centre uses the solar energy collected by the light-harvesting complex II to withdraw electrons from water, releasing oxygen into the atmosphere. It thus generates an electrochemical potential, providing the energy for carbon dioxide fixation and the synthesis of organic molecules, which make up the bulk of the biosphere1. The structure of the light-harvesting complex II has been determined at 3.4-Å resolution by electron crystallography2, but the high-resolution structure of the photosystem II reaction centre and other core components remained unknown. We have grown well-ordered two-dimensional crystals of a sub-core complex containing the reaction centre from spinach thylakoid membranes and used electron crystallography to obtain a projection map of its structure at 8-Å resolution. The features reveal the likely location of the key components that are active in electron transport, and suggest a structural homology and evolutionary links, not only with the purple bacterial reaction centre but also with the reaction centre of photosystem I.

Date: 1997
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DOI: 10.1038/39103

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