Moist and soft, dry and stiff: a review of neutron experiments on hydration-dynamics-activity relations in the purple membrane of Halobacterium salinarum.
Twenty-five years of neutron experiments on hydration and thermal dynamics in purple membranes of Halobacterium salinarum are reviewed. Neutron diffraction, elastic and quasielastic scattering, allowed to map the distribution of water and lipids and to measure thermal fluctuations and correlation times in the membranes, under various conditions of temperature, hydration and lipid environment. Strong correlations were established between dynamics parameters and the activity of bacteriorhodopsin (the purple membrane protein), as a light driven proton pump supporting the hypothesis that the influence of hydration on activity is in fact due to its effects on membrane thermal dynamics. Hydrogen-deuterium labelling experiments highlighted stiffer and softer parts in the bacteriorhodopsin structure. The soft parts would allow the conformational changes involved in activity, while the stiffer ones may control a valve-like function in vectorial proton transfer.
Zaccai
G
G
Institut de Biologie Structurale, Grenoble, France. zaccai@ibs.fr
D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism; D003903:Deuterium / Q000378:metabolism; D019617:Halobacterium salinarum / Q000737:chemistry*; D009502:Neutrons; D018717:Purple Membrane / Q000737:chemistry* / Q000378:metabolism*; D012542:Scattering, Radiation; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000378:metabolism*
D014867:Water; D001436:Bacteriorhodopsins; D003903:Deuterium