Catalysis of Ground State cis $$\rightarrow$$ → trans Isomerization of Bacteriorhodopsin’s Retinal Chromophore by a Hydrogen-Bond Network
Author:
Funder
Deutsche Forschungsgemeinschaft
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology,Biophysics
Link
http://link.springer.com/article/10.1007/s00232-018-0027-x/fulltext.html
Reference45 articles.
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2. Bondar A-N, Elstner M, Suhai S, Smith JC, Fischer S (2004) Mechanism of primary proton transfer in bacteriorhodopsin. Structure 12:1281–1288
3. Bondar A-N, Fischer S, Suhai S, Smith JC (2005a) Tuning of retinal twisting in bacteriorhodopsin controls the directionality of the early photocycle steps. J Phys Chem B 109:14786–14788
4. Bondar A-N, Smith JC, Fischer SK (2005b) QM/MM investigation of the hydrogen-bonding interactions in putative K and early-M intermediates of the bacteriorhodopsin photocycle. Phase Trans 78:671–675
5. Bondar A-N, Suhai S, Fischer S, Elstner M (2007) Suppression of the back proton-transfer from Asp85 to the retinal Schiff base in bacteriorhodopsin: a theoretical analysis of structural elements. J Struct Biol 157:454–469
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