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Characterization of a redox active cross-linked complex between cyanobacterial photosystem I and soluble ferredoxin.

1996; Springer Nature; Volume: 15; Issue: 9 Linguagem: Inglês

10.1002/j.1460-2075.1996.tb00569.x

1460-2075

Cécile Lelong, Egbert J. Boekema, Jochen Kruip, H. Bottin, Matthias Rögner, Pièrre Sétif,

Porphyrin and Phthalocyanine Chemistry

Research Article1 May 1996free access Characterization of a redox active cross-linked complex between cyanobacterial photosystem I and soluble ferredoxin. C. Lelong C. Lelong Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author E. J. Boekema E. J. Boekema Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author J. Kruip J. Kruip Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author H. Bottin H. Bottin Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author M. Rögner M. Rögner Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author P. Sétif P. Sétif Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author C. Lelong C. Lelong Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author E. J. Boekema E. J. Boekema Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author J. Kruip J. Kruip Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author H. Bottin H. Bottin Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author M. Rögner M. Rögner Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author P. Sétif P. Sétif Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. Search for more papers by this author Author Information C. Lelong1, E. J. Boekema1, J. Kruip1, H. Bottin1, M. Rögner1 and P. Sétif1 1Departement de Biologie Cellulaire et Moleculaire, Gif-sur- Yvette, France. The EMBO Journal (1996)15:2160-2168https://doi.org/10.1002/j.1460-2075.1996.tb00569.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info A covalent stoichiometric complex between photosystem I (PSI) and ferredoxin from the cyanobacterium Synechocystis sp. PCC 6803 was generated by chemical cross-linking. The photoreduction of ferredoxin, studied by laser flash absorption spectroscopy between 460 and 600 nm, is a fast process in 60% of the covalent complexes, which exhibit spectral and kinetic properties very similar to those observed with the free partners. Two major phases with t(1/2) <1 micros and approximately 10–14 micros are observed at two different pH values (5.8 and 8.0). The remaining complexes do not undergo fast ferredoxin reduction and 20–25% of the complexes are still able to reduce free ferredoxin or flavodoxin efficiently, thus indicating that ferredoxin is not bound properly in this proportion of covalent complexes. The docking site of ferredoxin on PSI was determined by electron microscopy in combination with image analysis. Ferredoxin binds to the cytoplasmic side of PSI, with its mass center 77 angstroms distant from the center of the trimer and in close contact with a ridge formed by the subunits PsaC, PsaD and PsaE. This docking site corresponds to a close proximity between the [2Fe- 2S] center of ferredoxin and the terminal [4Fe-4S] acceptor FII of PSI and is very similar in position to the docking site of flavodoxin, an alternative electron acceptor of PSI. Previous ArticleNext Article Volume 15Issue 91 May 1996In this issue RelatedDetailsLoading ...