Characterization of an isolated chloroplast membrane FeS protein and its identification as the photosystem I FeSA/FeSB binding protein

R. Max Wynn, Richard Malkin

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

An iron-sulfur protein of approx. 9 kDa has been isolated from spinach chloroplast membranes. Based on iron and sulfide content (∼900 nmol Fe and S2- per mg protein), optical absorbance and low-temperature EPR spectra, it appears that this protein contains 8Fe and 8S2- in two [4Fe4S] clusters. The protein cross-reacts with an antibody raised against a 9 kDa PS I subunit previously identified as the psaC (frxA) gene product. This identity was confirmed by the N-terminal amino acid sequence of the isolated FeS protein. It is concluded that the isolated FeS protein binds PS I centers FeSA and FeSB and that each of these centers contains 4Fe and 4S2-.

Original languageEnglish (US)
Pages (from-to)293-297
Number of pages5
JournalFEBS Letters
Volume229
Issue number2
DOIs
StatePublished - Mar 14 1988

Keywords

  • Iron-sulfur center
  • P700
  • Photosystem I, Ferredoxin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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