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J. Biol. Chem., Vol. 280, Issue 19, 18833-18841, May 13, 2005

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Structure of the Intermolecular Complex between Plastocyanin and Cytochrome f from Spinach^*

Francesco Musiani, Alexander Dikiy¶, Alexey Yu Semenov||, and Stefano Ciurli**

From the Laboratory of Bioinorganic Chemistry, Department of Agro-Environmental Science and Technology, University of Bologna, Viale Giuseppe Fanin 40, 40127 Bologna, Italy and ^||A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899 Moscow, Russia

In oxygenic photosynthesis, plastocyanin shuttles electrons between the membrane-bound complexes cytochrome b₆f and photosystem I. The homologous complex between cytochrome f and plastocyanin, both from spinach, is the object of this study. The solution structure of the reduced spinach plastocyanin was determined using high field NMR spectroscopy, whereas the model structure of oxidized cytochrome f was obtained by homology modeling calculations and molecular dynamics. The model structure of the intermolecular complex was calculated using the program AUTODOCK, taking into account biological information obtained from mutagenesis experiments. The best electron transfer pathway from the heme group of cytochrome f to the copper ion of plastocyanin was calculated using the program HARLEM, obtaining a coupling decay value of 1.8 x 10^–4. Possible mechanisms of interaction and electron transfer between plastocyanin and cytochrome f were discussed considering the possible formation of a supercomplex that associates one cytochrome b f₆, one photosystem I, and one plastocyanin.

Received for publication, November 11, 2004 , and in revised form, January 24, 2005.

^* This work was supported by INTAS Grant 01-483 (to S. C. and A. Y. S.), by the International Science and Technology Center Grant 2296 (to A. Y. S.), by Grants PRIN-2001 and PRIN-2003 from the Ministero Italiano dell'Università e della Ricerca (to S. C.), and by the Russian Foundation for Basic Research (Grant 03-04-48983) (to A. Y. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Table I and Fig. 1.

The atomic coordinates and structure factors (code 1YLB) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Recipient of fellowships provided by Consorzio Interuniversitario per le Risonanze Magnetiche di Metalloproteine Paramagnetiche (CIRMMP).

^¶ Present address: Dept. of Biotechnology, Norwegian University of Science and Technology, Trondheim, NO-7491, Norway.

^** To whom correspondence should be addressed: Dept. of Agro-Environmental Science and Technology, Laboratory of Bioinorganic Chemistry, University of Bologna, Viale Giuseppe Fanin 40, 40127 Bologna, Italy. Tel.: 39-051-209-6204; Fax: 39-051-209-6203; E-mail: stefano.ciurli{at}unibo.it.

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