Electron Transfer from the Rieske Iron-Sulfur Protein to Cytochrome F In
THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 277, No. 44, Issue of November 1, pp. 41865–41871, 2002 © 2002 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Electron Transfer from the Rieske Iron-Sulfur Protein (ISP) to Cytochrome f in Vitro IS A GUIDED TRAJECTORY OF THE ISP NECESSARY FOR COMPETENT DOCKING?* Received for publication, June 11, 2002, and in revised form, August 23, 2002 Published, JBC Papers in Press, August 30, 2002, DOI 10.1074/jbc.M205772200 Glenda M. Soriano‡§, Lian-Wang Guo¶**, Catherine de Vitryʈ, Toivo Kallas¶, and William A. Cramer‡§ From the ‡Department of Biological Sciences and Program in Biochemistry/Molecular Biology, Purdue University, West Lafayette, Indiana 47907-1392, the ¶Department of Biology and Microbiology, University of Wisconsin, Oshkosh, Wisconsin 54901, and ʈPhysiologie Membranaire et Mole´culaire du Chloroplaste, CNRS UPR 1261, Institute de Biologie Physico-Chimique, 75005 Paris, France 3 3 The time course of electron transfer in vitro between tochrome f plastocyanin or cytochrome c6 photosystem I soluble domains of the Rieske iron-sulfur protein (ISP) on the lumen (p-side) of the membrane, comprises the high and cytochrome f subunits of the cytochrome b6f com- potential electron transport chain of the plastoquinol oxidase, 3 plex of oxygenic photosynthesis was measured by whereas electron transfer between the two b-hemes, heme bp stopped-flow mixing. The domains were derived from heme bn, to a putative n-side bound quinone defines the low Chlamydomonas reinhardtii and expressed in Esche- potential chain. Absorption of a photon and charge separation richia coli.
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