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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons94115

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons93731

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

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Citation

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), 175-184. doi:10.1007/s11120-005-4117-0.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-9B6D-0
Abstract
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 β−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 Å 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