Bacteriorhodopsin as a model for proton pumps

According to a long-standing hypothesis, membrane pumps function by flip-flopping between two protein conformations that allow alternative access of the ion binding site to the two membrane surfaces. Site-specific mutagenesis, time-resolved spectroscopy and X-ray diffraction confirm this mechanism f...

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Bibliographic Details
Published in:Nature (London) 1995-06, Vol.375 (6531), p.461-463
Main Author: Lanyi, Janos K
Format: Article
Language:English
Subjects:
Bacteria
Bacteriorhodopsins - physiology
Biological and medical sciences
Cell membranes. Ionic channels. Membrane pores
Cell structures and functions
Electron Transport Complex IV - physiology
Fundamental and applied biological sciences. Psychology
Halobacterium
Humanities and Social Sciences
Ions
Membranes
Models, Biological
Molecular and cellular biology
multidisciplinary
progress
Protein Conformation
Proteins
Proton Pumps - physiology
Proton-Translocating ATPases - physiology
Protons
Science
Science (multidisciplinary)
Spectroscopy
X-ray diffraction
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Summary:According to a long-standing hypothesis, membrane pumps function by flip-flopping between two protein conformations that allow alternative access of the ion binding site to the two membrane surfaces. Site-specific mutagenesis, time-resolved spectroscopy and X-ray diffraction confirm this mechanism for bacteriorhodopsin, and implicate change of electrostatic interaction at the active site as the trigger for the global protein conformation change during the proton transport cycle.
ISSN:0028-0836
1476-4687
DOI:10.1038/375461a0