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The antenna system of photosystem II from Thermosynechococcus elongatus at 3.2 A resolution

MPG-Autoren
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Loll,  Bernhard
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kern,  Jana
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://link.springer.com/content/pdf/10.1007%2Fs11120-005-4117-0.pdf
(beliebiger Volltext)

https://doi.org/10.1007/s11120-005-4117-0
(beliebiger Volltext)

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Zitation

Loll, B., Kern, J., Zouni, A., Saenger, W., Biesiadka, J., & Irrgang, K. (2005). The antenna system of photosystem II from Thermosynechococcus elongatus at 3.2 A resolution. Photosynthesis Res., 86(1-2), 175-184. doi:10.1007/s11120-005-4117-0.


Zitierlink: https://hdl.handle.net/21.11116/0000-0002-510C-6
Zusammenfassung
The content and type of cofactors harboured in the Photosystem II core complex (PS IIcc) of the cyanobacterium Thermosynechococcus elongatus has been determined by biochemical and spectroscopic methods. 17 +/- 1 chlorophyll a per pheophytin a and 0.25 beta-carotene per chlorophyll a have been found in re-dissolved crystals of dimeric PS IIcc. The X-ray crystal structure of PS IIcc from Thermosynechococcus elongatus at 3.2 A resolution clearly shows chlorophyll a molecules arranged in two layers close to the cytoplasmic and lumenal sides of the thylakoid membrane. Each of the cytoplasmic layers contains 9 chlorophyll a, whose positions and orientations are related by a local twofold rotation pseudo-C2 axis passing through the non-haem Fe2+. These chlorophyll a are arranged comparably to those in the antenna domains of PsaA and PsaB of cyanobacterial Photosystem I affirming an evolutionary relation. The chlorophyll a in the lumenal layer are less well conserved between Photosystems I and II and even between CP43 and CP47 with 4 chlorophyll a in the former and 7 in the latter.