Cross-linking of transmembrane helices reveals a rigid-body mechanism in bacteriorhodopsin transport

Rosana Simón-Vázquez, Tzvetana Lazarova, Alex Perálvarez-Marín, José Luis Bourdelande, Esteve Padrós

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4 Citations (Scopus)

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 wildtype bacteriorhodopsin (gray traces). If helices F and C 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 rigidbody mechanism of bacteriorhodopsin proton transport. © 2009 WNey-VCH Verlag GmbH & Co. KGaA.
Original languageEnglish
Pages (from-to)8523-8525
JournalAngewandte Chemie - International Edition
Volume48
Issue number45
DOIs
Publication statusPublished - 26 Oct 2009

Keywords

  • Bacteriorhodopsin
  • Helical structures
  • Membrane proteins
  • Proton transport
  • Structural biology

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