Shahab Rouhani

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The structure of an early M-intermediate of the wild-type bacteriorhodopsin photocycle formed by actinic illumination at 230 K has been determined by x-ray crystallography to a resolution of 2.0 A. Three-dimensional crystals were trapped by illuminating with actinic light at 230 K, followed by quenching in liquid nitrogen. Amide I, amide II, and other(More)
Despite extensive investigation, the precise mechanism controlling the opening of the cytoplasmic proton uptake pathway in bacteriorhodopsin (bR) has remained a mystery. From an analysis of the X-ray structure of the D96G/F171C/F219L triple mutant of bR and 60 independent molecular dynamics simulations of bR photointermediates, we report that the(More)
Bacteriorhodopsin (bR) is the sole protein component of the purple membrane of Halobacterium salinarium 1. The function of bR in vivo is to convert solar energy into a pH gradient across the cell membrane which the organism uses to drive ATP synthesis 2. Bacteriorhodopsin undergoes a light-induced cycle of physicochemical changes for for every proton it(More)
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