title: Structural and energetic determinants of primary proton transfer in bacteriorhodopsin.
abstract: In the light-driven bacteriorhodopsin proton pump, the first proton transfer step is from the retinal Schiff base to a nearby carboxylate group. The mechanism of this transfer step is highly controversial, in particular whether a direct proton jump is allowed. Here, we review the structural and energetic determinants of the direct proton transfer path computed by using a combined quantum mechanical/molecular mechanical approach. Both protein flexibility and electrostatic interactions play an important role in shaping the proton transfer energy profile. Detailed analysis of the energetics of putative transitions in the first half of the photocycle focuses on two elements that determine the likelihood that a given configuration of the active site is populated during the proton-pumping cycle. First, the rate-limiting barrier for proton transfer must be consistent with the kinetics of the photocycle. Second, the active-site configuration must be compatible with a productive overall pumping cycle.
authors.affiliation: Computational Molecular Biophysics, IWR, Heidelberg University, Im Neuenheimer Feld 368, Heidelberg, Germany.
authors.forename: Ana-Nicoleta
authors.initials: AN
authors.lastname: Bondar
authors.forename: Jeremy C
authors.initials: JC
authors.lastname: Smith
authors.forename: Stefan
authors.initials: S
authors.lastname: Fischer
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry*; D003198:Computer Simulation; D017136:Ion Transport; D011522:Protons; D011789:Quantum Theory; D055672:Static Electricity
chemical_list: D011522:Protons; D001436:Bacteriorhodopsins