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J Photochem Photobiol B. 2016 Jul;160:347-54. doi: 10.1016/j.jphotobiol.2016.04.030. Epub 2016 Apr 30.

Photoreduction of the ferredoxin/ferredoxin-NADP(+)-reductase complex by a linked ruthenium polypyridyl chromophore.

Author information

1
CEA, iBiTec-S/SB2SM, CEA Saclay, 91191 Gif sur Yvette, France; Université Paris-Saclay, I2BC, UMR 9198, 91190 Gif sur Yvette, France.
2
CEA, iBiTec-S/SB2SM, CEA Saclay, 91191 Gif sur Yvette, France.
3
CEA, iBiTec-S/SB2SM, CEA Saclay, 91191 Gif sur Yvette, France; Université Paris-Saclay, I2BC, UMR 9198, 91190 Gif sur Yvette, France. Electronic address: pierre.setif@cea.fr.

Abstract

Photosynthetic ferredoxin and its main partner ferredoxin-NADP(+)-reductase (FNR) are key proteins during the photoproduction of reductive power involved in photosynthetic growth. In this work, we used covalent attachment of ruthenium derivatives to different cysteine mutants of ferredoxin to trigger by laser-flash excitation both ferredoxin reduction and subsequent electron transfer from reduced ferredoxin to FNR. Rates and yields of reduction of the ferredoxin [2Fe-2S] cluster by reductively quenched Ru* could be measured for the first time for such a low redox potential protein whereas ferredoxin-FNR electron transfer was characterized in detail for one particular Ru-ferredoxin covalent adduct. For this adduct, the efficiency of FNR single reduction by reduced ferredoxin was close to 100% under both first-order and diffusion-limited second-order conditions. Interprotein intracomplex electron transfer was measured unambiguously for the first time with a fast rate of c. 6500s(-1). Our measurements point out that Ru photosensitizing is a powerful approach to study the functional interactions of ferredoxin with its numerous partners besides FNR.

KEYWORDS:

Electron transfer; Kinetics; Photochemistry; Photosynthesis; Protein–protein interactions

[Indexed for MEDLINE]

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