Communication

Cross-Linking of Transmembrane Helices Reveals a Rigid-Body Mechanism in Bacteriorhodopsin Transport†

  1. Rosana Simón-Vázquez Dr.1,
  2. Tzvetana Lazarova Dr.1,
  3. Alex Perálvarez-Marín Dr.1,3,
  4. José-Luis Bourdelande Dr.2,
  5. Esteve Padrós Dr.1

Article first published online: 6 OCT 2009

DOI: 10.1002/anie.200904031

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 48, Issue 45, pages 8523–8525, October 26, 2009

Additional Information

How to Cite

Simón-Vázquez, R., Lazarova, T., Perálvarez-Marín, A., Bourdelande, J.-L. and Padrós, E. (2009), Cross-Linking of Transmembrane Helices Reveals a Rigid-Body Mechanism in Bacteriorhodopsin Transport. Angew. Chem. Int. Ed., 48: 8523–8525. doi: 10.1002/anie.200904031

Author Information

  1. 1

    Unitat de Biofísica, Departament de Bioquímica i de Biologia Molecular and Centre d'Estudis en Biofísica, Facultat de Medicina, Universitat Autònoma de Barcelona, 08193 Bellaterra (Spain)

  2. 2

    Departament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra (Spain)

  3. 3

    Current address:, Brigham and Women's Hospital, Francis St. 75, Boston, MA 02115 (USA)

  1. †

    We thank Dr. Víctor Lórenz-Fonfría and Dr. Pere Garriga for helpful discussions, Dr. Enric Querol for advice at the beginning of this work, Jordi Hernando for help in the flash photolysis experiments, Elodia Serrano and Neus Ontiveros for excellent technical assistance, and Dr. Mathias Lübben (Ruhr-Universität Bochum) for providing the pEF191 vector and the MPK409 strain. This work was supported by a Direcció General de Recerca fellowship (2007PIV10038) to T.L. and by a Dirección General de Investigación grant (BFU2006-04656/BMC).

Publication History

  1. Issue published online: 20 OCT 2009
  2. Article first published online: 6 OCT 2009
  3. Manuscript Received: 21 JUL 2009

Funded by

  • Dirección General de Investigación. Grant Number: BFU2006-04656/BMC

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Keywords:

  • bacteriorhodopsin;
  • helical structures;
  • membrane proteins;
  • proton transport;
  • structural biology
Thumbnail image of graphical abstract

A flashy protein: The flash-induced transient protonation of pyranine has been studied in the presence of the cross-linked double mutant E166C/A228C (red trace), a reduced mutant (blue trace), and wild-type bacteriorhodopsin (gray traces). If helices F and G are cross-linked, there is a delay in both proton release (extracellular side) and proton uptake (cytoplasmic side). Together with flash photolysis and FTIR studies, these data support a rigid-body mechanism of bacteriorhodopsin proton transport.

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