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

doi:10.1002/anie.200904031

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

Research output: Contribution to journal › Article › Research › peer-review

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 language	English
Pages (from-to)	8523-8525
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	45
DOIs	https://doi.org/10.1002/anie.200904031
Publication status	Published - 26 Oct 2009

Keywords

Bacteriorhodopsin
Helical structures
Membrane proteins
Proton transport
Structural biology

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title = "Cross-linking of transmembrane helices reveals a rigid-body mechanism in bacteriorhodopsin transport",

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. {\textcopyright} 2009 WNey-VCH Verlag GmbH & Co. KGaA.",

keywords = "Bacteriorhodopsin, Helical structures, Membrane proteins, Proton transport, Structural biology",

author = "Rosana Sim{\'o}n-V{\'a}zquez and Tzvetana Lazarova and Alex Per{\'a}lvarez-Mar{\'i}n and Bourdelande, {Jos{\'e} Luis} and Esteve Padr{\'o}s",

year = "2009",

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day = "26",

doi = "10.1002/anie.200904031",

language = "English",

volume = "48",

pages = "8523--8525",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley and Sons Ltd",

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Cross-linking of transmembrane helices reveals a rigid-body mechanism in bacteriorhodopsin transport. / Simón-Vázquez, Rosana; Lazarova, Tzvetana; Perálvarez-Marín, Alex ; Bourdelande, José Luis; Padrós, Esteve.

In: Angewandte Chemie - International Edition, Vol. 48, No. 45, 26.10.2009, p. 8523-8525.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Cross-linking of transmembrane helices reveals a rigid-body mechanism in bacteriorhodopsin transport

AU - Simón-Vázquez, Rosana

AU - Lazarova, Tzvetana

AU - Perálvarez-Marín, Alex

AU - Bourdelande, José Luis

AU - Padrós, Esteve

PY - 2009/10/26

Y1 - 2009/10/26

N2 - 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.

AB - 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.

KW - Bacteriorhodopsin

KW - Helical structures

KW - Membrane proteins

KW - Proton transport

KW - Structural biology

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EP - 8525

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

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