Abstract
Annual Review of Biophysics and Biomolecular Structure
Vol. 28:
367-399
(Volume publication date June 1999)
(doi:10.1146/annurev.biophys.28.1.367)
CLOSING IN ON BACTERIORHODOPSIN: Progress in Understanding the Molecule Ulrich Haupts, Jörg Tittor, and Dieter OesterheltMax-Planck-Institut für Biochemie, Martinsried, D82152 Germany; e-mail: tittor@biochem.mpg.de ▪ Abstract Bacteriorhodopsin is the best understood ion transport protein and has become a paradigm for membrane proteins in general and transporters in particular. Models up to 2.5 Å resolution of bacteriorhodopsin's structure have been published during the last three years and are basic for understanding its function. Thus one focus of this review is to summarize and to compare these models in detail. Another focus is to follow the protein through its catalytic cycle in summarizing more recent developments. We focus on literature published since 1995; a comprehensive series of reviews was published in 1995 (112). Most recent citing papers (via CrossRef)Control of retinal isomerization in bacteriorhodopsin in the high-intensity regime Proceedings of the National Academy of Sciences 106(27):10896-10900 (2009) Determination of protein structural flexibility by microsecond force spectroscopy Nature Nanotechnology (2009) Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues Proceedings of the National Academy of Sciences 106(19):7718-7723 (2009) Water-mediated Spectral Shifts in Rhodopsin and Bathorhodopsin Photochemistry and Photobiology 85(2):517-520 (2009) Spectral Signatures of the Pentagonal Water Cluster in Bacteriorhodopsin ChemPhysChem 9(18):2703-2707 (2009)
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