TY - JOUR
T1 - Three-dimensional structure of photosystem II
AU - Holzenburg, Andreas
AU - Bewley, Maria C.
AU - Wilson, Fiona H.
AU - Nicholson, William V.
AU - Ford, Robert C.
PY - 1993
Y1 - 1993
N2 - THE photosynthetic oxidation of water occurs within a multi-protein complex called photosystem II (PSII), located in the thylakoid membranes of plants and cyanobacteria. Little information on PSII architecture is available; even the oligomeric nature of the complex is contentious, with various predictions of monomeric1, dimeric and tetrameric2-4 forms. Biochemistry suggests that it consists of an outer shell of easily removable light-harvesting proteins and a more resistant core5. The core itself can be split into further light-harvesting proteins and a reaction centre5,6. The reaction centre polypeptides bind the electron transfer components, and probably contain amino-acid residues liganded to the cluster of four Mn atoms that is believed to constitute the water 'splitting' site6-8. We report here the first, to our knowledge, three-dimensional functionally intact structure of PSII of higher plants, complete with antennae and core light-harvesting proteins. Our model has been obtained by digital image processing of ordered two-dimensional arrays of the complex, such as have often been observed 4,9-12.
AB - THE photosynthetic oxidation of water occurs within a multi-protein complex called photosystem II (PSII), located in the thylakoid membranes of plants and cyanobacteria. Little information on PSII architecture is available; even the oligomeric nature of the complex is contentious, with various predictions of monomeric1, dimeric and tetrameric2-4 forms. Biochemistry suggests that it consists of an outer shell of easily removable light-harvesting proteins and a more resistant core5. The core itself can be split into further light-harvesting proteins and a reaction centre5,6. The reaction centre polypeptides bind the electron transfer components, and probably contain amino-acid residues liganded to the cluster of four Mn atoms that is believed to constitute the water 'splitting' site6-8. We report here the first, to our knowledge, three-dimensional functionally intact structure of PSII of higher plants, complete with antennae and core light-harvesting proteins. Our model has been obtained by digital image processing of ordered two-dimensional arrays of the complex, such as have often been observed 4,9-12.
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U2 - 10.1038/363470a0
DO - 10.1038/363470a0
M3 - Article
AN - SCOPUS:0027157307
SN - 0028-0836
VL - 363
SP - 470
EP - 472
JO - Nature
JF - Nature
IS - 6428
ER -