Structure of photosystem I

Petra Fromme, Patrick Jordan, Norbert Krauß

Research output: Contribution to journalReview articlepeer-review

384 Scopus citations


In plants and cyanobacteria, the primary step in oxygenic photosynthesis, the light induced charge separation, is driven by two large membrane intrinsic protein complexes, the photosystems I and II. Photosystem I catalyses the light driven electron transfer from plastocyanin/cytochrome c6 on the lumenal side of the membrane to ferredoxin/flavodoxin at the stromal side by a chain of electron carriers. Photosystem I of Synechococcus elongatus consists of 12 protein subunits, 96 chlorophyll a molecules, 22 carotenoids, three [4Fe4S] clusters and two phylloquinones. Furthermore, it has been discovered that four lipids are intrinsic components of photosystem I. Photosystem I exists as a trimer in the native membrane with a molecular mass of 1068 kDa for the whole complex. The X-ray structure of photosystem I at a resolution of 2.5 Å shows the location of the individual subunits and cofactors and provides new information on the protein-cofactor interactions. [P. Jordan, P. Fromme, H.T. Witt, O. Klukas, W. Saenger, N. Krauß, Nature 411 (2001) 909-917]. In this review, biochemical data and results of biophysical investigations are discussed with respect to the X-ray crystallographic structure in order to give an overview of the structure and function of this large membrane protein.

Original languageEnglish (US)
Pages (from-to)5-31
Number of pages27
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number1-3
StatePublished - Oct 30 2001
Externally publishedYes


  • Core antenna
  • Electron transfer chain
  • Membrane protein
  • Photosystem I
  • Structure
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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