Discovery of native metal ion sites located on the ferredoxin docking side of photosystem I

Lisa M. Utschig, Lin X. Chen, Oleg G. Poluektov

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Photosystem I (PSI) is a large membrane protein that catalyzes light-driven electron transfer across the thylakoid membrane from plastocyanin located in the lumen to ferredoxin in the stroma. Metal analysis reveals that PSI isolated from the cyanobacterial membranes of Synechococcus leopoliensis has a near-stoichiometric 1 molar equiv of Zn2+ per PSI monomer and two additional surface metal ion sites that favor Cu2+ binding. Two-dimensional hyperfine sublevel correlation (HYSCORE) spectroscopy reveals coupling to the so-called remote nitrogen of a single histidine coordinated to one of the Cu2+ centers. EPR and X-ray absorption fine structure (XAFS) studies of 2Cu-PSI complexes reveal the direct interaction of ferredoxin with the Cu2+ centers on PSI, establishing the location of native metal sites on the ferredoxin docking side of PSI. On the basis of these spectroscopic results and previously reported site-directed mutagenesis studies, inspection of the PSI crystal structure reveals a cluster of three highly conserved residues, His(D95), Glu(D103), and Asp(C23), as a likely Cu 2+ binding site. The discovery of surface metal sites on the acceptor side of PSI provides a unique opportunity to probe the stromal region of PSI and the interactions of PSI with its reaction partner, the soluble electron carrier protein ferredoxin.

Original languageEnglish (US)
Pages (from-to)3671-3676
Number of pages6
JournalBiochemistry
Volume47
Issue number12
DOIs
StatePublished - Mar 25 2008

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)

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