Three-dimensional structure of photosystem II

Andreas Holzenburg, Maria C. Bewley, Fiona H. Wilson, William V. Nicholson, Robert C. Ford

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

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
Original languageEnglish
Pages (from-to)470-472
Number of pages3
JournalNature
Volume363
DOIs
Publication statusPublished - 3 Jun 1993

Fingerprint

photosystem II
multiprotein complexes
proteins
digital images
thylakoids
biochemistry
antennae
electron transfer
Cyanobacteria
polypeptides
water
image analysis
oxidation
amino acids
prediction

Cite this

Holzenburg, A., Bewley, M. C., Wilson, F. H., Nicholson, W. V., & Ford, R. C. (1993). Three-dimensional structure of photosystem II. Nature, 363, 470-472. https://doi.org/10.1038/363470a0
Holzenburg, Andreas ; Bewley, Maria C. ; Wilson, Fiona H. ; Nicholson, William V. ; Ford, Robert C. / Three-dimensional structure of photosystem II. In: Nature. 1993 ; Vol. 363. pp. 470-472.
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abstract = "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",
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Holzenburg, A, Bewley, MC, Wilson, FH, Nicholson, WV & Ford, RC 1993, 'Three-dimensional structure of photosystem II', Nature, vol. 363, pp. 470-472. https://doi.org/10.1038/363470a0

Three-dimensional structure of photosystem II. / Holzenburg, Andreas; Bewley, Maria C.; Wilson, Fiona H.; Nicholson, William V.; Ford, Robert C.

In: Nature, Vol. 363, 03.06.1993, p. 470-472.

Research output: Contribution to journalArticle

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AU - Wilson, Fiona H.

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AU - Ford, Robert C.

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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

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Holzenburg A, Bewley MC, Wilson FH, Nicholson WV, Ford RC. Three-dimensional structure of photosystem II. Nature. 1993 Jun 3;363:470-472. https://doi.org/10.1038/363470a0