help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Originally published as Biophys J. BioFAST on September 1, 2006.
doi:10.1529/biophysj.106.083709
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
biophysj.106.083709v1
91/10/3707    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Scheuring, S.
Right arrow Articles by Sturgis, J. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Scheuring, S.
Right arrow Articles by Sturgis, J. N.
Biophysical Journal 91:3707-3717 (2006)
© 2006 The Biophysical Society

Dynamics and Diffusion in Photosynthetic Membranes from Rhodospirillum Photometricum

Simon Scheuring * and James N. Sturgis {dagger}

* Institut Curie, Unite Mixte de Recherche-Centre National de Recherche Scientifique 168, 75231 Paris Cedex 05, France; and {dagger} Laboratoire d'Ingenierie de Systemes Macromoleculaire, Institute de Biologie Structurale et Microbiologie, Centre National de Recherche Scientifique, 13402 Marseille Cedex 20, France

Correspondence: Address reprint requests to James N. Sturgis, Tel.: 33-4-91164485; Fax: 33-4-91712124; E-mail: sturgis{at}ibsm.cnrs-mrs.fr.

Photosynthetic organisms drive their metabolism by converting light energy into an electrochemical gradient with high efficiency. This conversion depends on the diffusion of quinones within the membrane. In purple photosynthetic bacteria, quinones reduced by the reaction center (RC) diffuse to the cytochrome bc1 complex and then return once reoxidized to the RC. In Rhodospirillum photometricum the RC-containing core complexes are found in a disordered molecular environment, with fixed light-harvesting complex/core complex ratio but without a fixed architecture, whereas additional light-harvesting complexes synthesized under low-light conditions pack into large paracrystalline antenna domains. Here, we have analyzed, using time-lapse atomic force microscopy, the dynamics of the protein complexes in the different membrane domains and find that the disordered regions are dynamic whereas ordered antennae domains are static. Based on our observations we propose, and analyze using Monte Carlo simulations, a model for quinone diffusion in photosynthetic membranes. We show that the formation of large static antennae domains may represent a strategy for increasing electron transfer rates between distant complexes within the membrane and thus be important for photosynthetic efficiency.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2006 by the Biophysical Society.