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Issue 6, 2006
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Structural and energetic determinants of primary proton transfer in bacteriorhodopsin

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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 focusses 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.

Graphical abstract: Structural and energetic determinants of primary proton transfer in bacteriorhodopsin

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Publication details

The article was received on 21 Nov 2005, accepted on 20 Mar 2006 and first published on 04 Apr 2006


Article type: Perspective
DOI: 10.1039/B516451F
Citation: Photochem. Photobiol. Sci., 2006,5, 547-552
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    Structural and energetic determinants of primary proton transfer in bacteriorhodopsin

    A. Bondar, J. C. Smith and S. Fischer, Photochem. Photobiol. Sci., 2006, 5, 547
    DOI: 10.1039/B516451F

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