PMID: 2505837Jun 27, 1989Paper

Structural and functional properties of the cyanobacterial photosystem I complex

Biochemistry
R M WynnR Malkin

Abstract

Photosystem I (PSI) complexes have been isolated from two cyanobacterial strains, Synechococcus sp. PCC 7002 and 6301. These complexes contain six to seven low molecular mass subunits in addition to the two high molecular mass subunits previously shown to bind the primary reaction center components. Chemical cross-linking of ferredoxin to the complex identified a 17.5-kDa subunit as the ferredoxin-binding protein in the Synechococcus sp. PCC 6301-PSI complex. The amino acid sequence of this subunit, deduced from the DNA sequence of the gene, confirmed its identity as the psaD gene product. A 17-kDa subunit cross-links to the electron donor, cytochrome c-553, in a manner analogous to the cross-linking of plastocyanin to the higher plant PSI complex. Using antibodies raised against the spinach psaC gene product (a 9-kDa subunit which binds Fe-S centers A and B), we identified an analogous protein in the cyanobacterial PSI complex.

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Citations

May 1, 1995·Photosynthesis Research·P R ChitnisR Nechushtai
Feb 1, 1994·Journal of Bioenergetics and Biomembranes·M R RedinboS Merchant
Jan 22, 1991·Biochimica Et Biophysica Acta·D B Knaff, M Hirasawa
Mar 12, 2004·Annual Review of Plant Physiology and Plant Molecular Biology·Cheryl A. Kerfeld, David W. Krogmann
Jul 1, 1991·Journal of Basic and Clinical Physiology and Pharmacology·O AlmogR Nechushtai
Oct 24, 1998·Biochimica Et Biophysica Acta·M HipplerJ D Rochaix
Jan 14, 2004·Journal of Plant Physiology·M Dolores MiramarM Luisa Peleato
Mar 29, 1991·Biochemical and Biophysical Research Communications·G D HitchensC O Patterson
Nov 1, 2001·Biochimica Et Biophysica Acta·P Sétif
Aug 3, 2001·The Journal of Biological Chemistry·H ZhangW A Cramer

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