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Science 8 March 2002:
Vol. 295. no. 5561, pp. 1842 - 1843
DOI: 10.1126/science.1070366
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Perspectives

STRUCTURAL BIOLOGY:
PMF Through the Redox Loop

David Richardson and Gary Sawers

Mitchell's chemiosmotic theory of energy coupling may have won him the Nobel Prize, but scientists are still pondering how the transmembrane proton gradient he postulated is generated. In their Perspective, Richardson and Sawers discuss the newly resolved structure of a bacterial respiratory enzyme (Jormakka et al.), which reveals that the proton electrochemical gradient could be generated through a redox loop.

D. Richardson is at the School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. E-mail: d.richardson{at}uea.ac.uk G. Sawers is in the Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK. E-mail: gary.sawers{at}bbsrc.ac.uk

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Characterization of Protein-Protein Interactions Involved in Iron Reduction by Shewanella oneidensis MR-1.
D. E. Ross, S. S. Ruebush, S. L. Brantley, R. S. Hartshorne, T. A. Clarke, D. J. Richardson, and M. Tien (2007)
Appl. Envir. Microbiol. 73, 5797-5808
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Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.
C. R. D. Lancaster, U. S. Sauer, R. Gross, A. H. Haas, J. Graf, H. Schwalbe, W. Mantele, J. Simon, and M. G. Madej (2005)
PNAS 102, 18860-18865
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Characterization of the Menaquinone Reduction Site in the Diheme Cytochrome b Membrane Anchor of Wolinella succinogenes NiFe-hydrogenase.
R. Gross, R. Pisa, M. Sanger, C. R. D. Lancaster, and J. Simon (2004)
J. Biol. Chem. 279, 274-281
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