title: Water and bacteriorhodopsin: structure, dynamics, and function.
abstract: A wealth of information has been gathered during the past decades that water molecules do play an important role in the structure, dynamics, and function of bacteriorhodopsin (bR) and purple membrane. Light-induced structural alterations in bR as detected by X-ray and neutron diffraction at low and high resolution are discussed in relationship to the mechanism of proton pumping. The analysis of high resolution intermediate structures revealed photon-induced rearrangements of water molecules and hydrogen bonds concomitant with conformational changes in the chromophore and the protein. These observations led to an understanding of key features of the pumping mechanism, especially the vectoriality and the different modes of proton translocation in the proton release and uptake domain of bR. In addition, water molecules influence the function of bR via equilibrium fluctuations, which must occur with adequate amplitude so that energy barriers between conformational states can be overcome.
authors.affiliation: Technische Universität Darmstadt, Institute of Biochemistry, Physical Biochemistry, Petersenstrasse 22, D-64287 Darmstadt, Germany. dencher@pop.tu-darmstadt.de
authors.forename: N A
authors.initials: NA
authors.lastname: Dencher
authors.forename: H J
authors.initials: HJ
authors.lastname: Sass
authors.forename: G
authors.initials: G
authors.lastname: Büldt
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry*; D003461:Crystallography; D008956:Models, Chemical; D010777:Photochemistry; D011487:Protein Conformation; D017494:Proton Pumps / Q000737:chemistry; D018717:Purple Membrane / Q000737:chemistry; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D017494:Proton Pumps; D014867:Water; D001436:Bacteriorhodopsins