Three-dimensional structure of the plant photosystem II reaction centre at 8 Å resolution

Kyong-Hi Rhee, Edward P. Morris, James Barber () and Werner Kühlbrandt ()
Additional contact information
Kyong-Hi Rhee: Max-Planck-Institut für Biophysik
Edward P. Morris: Wolfson Laboratories, Imperial College of Science, Technology & Medicine
James Barber: Wolfson Laboratories, Imperial College of Science, Technology & Medicine
Werner Kühlbrandt: Max-Planck-Institut für Biophysik

Nature, 1998, vol. 396, issue 6708, 283-286

Abstract: 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 oxygen1. 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 has a relative molecular mass of 160K, can perform light-mediated energy and electron-transfer reactions but is unable to oxidize water2. The complex contains 23 transmembrane α-helices, of which 16 have been assigned to the D1, D2 and CP47 proteins. The arrangement of these helices is remarkably similar to that of the helices in the reaction centres of purple bacteria and of plant photosystem I, indicating a common evolutionary origin for these assemblies. The map suggests that redox cofactors in the D1–D2 complex are located in positions analogous to those in the bacterial reaction centre, but the distance between the chlorophylls corresponding to the bacterial ‘special pair’ is significantly larger.

Date: 1998
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/24421 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:396:y:1998:i:6708:d:10.1038_24421

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/24421

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().