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

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 bot...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2009-10, Vol.48 (45), p.8523-8525
Main Authors: Simón-Vázquez, Rosana, Lazarova, Tzvetana, Perálvarez-Marín, Alex, Bourdelande, José-Luis, Padrós, Esteve
Format: Article
Language:English
Subjects:
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Bacteriorhodopsin
Bacteriorhodopsins - chemistry
Bacteriorhodopsins - metabolism
Cross-Linking Reagents - chemistry
Cross-Linking Reagents - pharmacology
Crosslinking
Delay
Flash photolysis
helical structures
Helices
Kinetics
membrane proteins
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Membrane Transport Proteins - chemistry
Protein Conformation
Proteins
proton transport
structural biology
Transport
Uptakes
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200904031