Cross‐Linking of Transmembrane Helices Reveals a Rigid‐Body Mechanism in Bacteriorhodopsin Transport | Zendy

SimónVázquez Rosana | Zendy; Lazarova Tzvetana | Zendy; PerálvarezMarín Alex | Zendy; Bourdelande JoséLuis | Zendy; Padrós Esteve | Zendy

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

Author(s) -

SimónVázquez Rosana,

Lazarova Tzvetana,

PerálvarezMarín Alex,

Bourdelande JoséLuis,

Padrós Esteve

Publication year - 2009

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200904031

Subject(s) - bacteriorhodopsin , protonation , chemistry , proton , flash photolysis , proton transport , biophysics , crystallography , stereochemistry , physics , biochemistry , membrane , ion , kinetics , biology , nuclear physics , organic chemistry , quantum mechanics , reaction rate constant

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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