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J Biol Chem, Vol. 274, Issue 47, 33565-33570, November 19, 1999

Site-directed Mutagenesis of Cytochrome c₆ from Anabaena Species PCC 7119
IDENTIFICATION OF SURFACE RESIDUES OF THE HEMEPROTEIN INVOLVED IN PHOTOSYSTEM I REDUCTION

From the Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla y Consejo Superior de Investigaciones Científicas, Centro Isla de la Cartuja, Américo Vespucio s/n, 41092 Sevilla, Spain

A number of surface residues of cytochrome c₆ from the cyanobacterium Anabaena sp. PCC 7119 have been modified by site-directed mutagenesis. Changes were made in six amino acids, two near the heme group (Val-25 and Lys-29) and four in the positively charged patch (Lys-62, Arg-64, Lys-66, and Asp-72). The reactivity of mutants toward the membrane-anchored complex photosystem I was analyzed by laser flash absorption spectroscopy. The experimental results indicate that cytochrome c₆ possesses two areas involved in the redox interaction with photosystem I: 1) a positively charged patch that may drive its electrostatic attractive movement toward photosystem I to form a transient complex and 2) a hydrophobic region at the edge of the heme pocket that may provide the contact surface for the transfer of electrons to P₇₀₀. The isofunctionality of these two areas with those found in plastocyanin (which acts as an alternative electron carrier playing the same role as cytochrome c₆) are evident.

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