1998
DOI: 10.1038/24421
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Three-dimensional structure of the plant photosystem II reaction centre at 8 Å resolution

Abstract: Photosystem II is a multisubunit enzyme complex involved in plant photosynthesis. It uses solar energy to catalyse the breakdown of water to reducing equivalents and molecular oxygen. Native photosystem II comprises more than 25 different subunits, and has a relative molecular mass of more than 600K. Here we report the three-dimensional structure of a photosystem II subcomplex, containing the proteins D1, D2, CP47 and cytochrome b-559, determined by electron crystallography. This CP47 reaction centre, which ha… Show more

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Cited by 340 publications
(316 citation statements)
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“…This observation is consistent with the estimated 10 Å center to center distance between the metal centers of these chlorophylls from electron and X-ray diffraction studies of PSII crystals (17,18,73) as opposed to the 7.6 Å found in bacterial reaction centers (3)(4)(5).…”
Section: Location Of 3 P As a Function Of Temperaturesupporting
confidence: 88%
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“…This observation is consistent with the estimated 10 Å center to center distance between the metal centers of these chlorophylls from electron and X-ray diffraction studies of PSII crystals (17,18,73) as opposed to the 7.6 Å found in bacterial reaction centers (3)(4)(5).…”
Section: Location Of 3 P As a Function Of Temperaturesupporting
confidence: 88%
“…(3) In the bacterial reaction centers the electrochromic shift of the accessory chlorophyll (B A , B B , or both) accompanying the oxidation of the primary donor is to the blue (96,97). Because of the similar orientation of the reaction center chlorophylls to those of the bacterial reaction centers (3,5,8,9,10,17,18,98), we expect a similar blue shift in PSII if the cation were localized on P A + . If the cation were localized on B A , then because of the closeness of ring I of P B to B A + , there would likely be an electrochromic shift of P B which would be insensitive to the D1-198 mutations.…”
Section: Location Of 3 P As a Function Of Temperaturementioning
confidence: 97%
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“…These studies relied on mild detergent solubilization procedures and refined electron microscopy analysis, including single particle averaging (Boekema et al, 1999), cryoelectron microscopy (Nield et al, 2000), and two-dimensional crystal electron diffraction (Rhee et al, 1998;Barber and Kuhlbrandt, 1999;Hankamer et al, 1999). Various PSII forms were observed, ranging from a large protein complex retaining its peripheral antenna complement to subcore particles.…”
Section: Discussionmentioning
confidence: 99%
“…It had been shown by electron microscopy (EM) that the PSIIRC core complex of plants and cyanobacteria is dimeric (reviewed in Hankamer et al 1997). In fact, our early EM studies employing both electron crystallography (Rhee et al 1997(Rhee et al , 1998Hankamer et al 1999Hankamer et al , 2001) and single particle analyses (Nield et al 2000a(Nield et al ,b, 2002 had also revealed the relative positions of the D1, D2, CP43 and CP47 proteins within each monomer of the dimeric PSII RC core complex isolated from higher plants (spinach) and suggested how their transmembrane helices were arranged (Barber 2002). The best resolution obtained was 8 Å and thus densities could be tentatively assigned to Chls bound within the CP47 protein as well as those that were contained within the D1/D2 heterodimer (Rhee et al 1998).…”
Section: The Structure Of Psii and Its Oecmentioning
confidence: 99%