Protonation reactions and their coupling in bacteriorhodopsin.
Light-induced changes of the proton affinities of amino acid side groups are the driving force for proton translocation in bacteriorhodopsin. Recent progress in obtaining structures of bacteriorhodopsin and its intermediates with an increasingly higher resolution, together with functional studies utilizing mutant pigments and spectroscopic methods, have provided important information on the molecular architecture of the proton transfer pathways and the key groups involved in proton transport. In the present paper I consider mechanisms of light-induced proton release and uptake and intramolecular proton transport and mechanisms of modulation of proton affinities of key groups in the framework of these data. Special attention is given to some important aspects that have surfaced recently. These are the coupling of protonation states of groups involved in proton transport, the complex titration of the counterion to the Schiff base and its origin, the role of the transient protonation of buried groups in catalysis of the chromophore's thermal isomerization, and the relationship between proton affinities of the groups and the pH dependencies of the rate constants of the photocycle and proton transfer reactions.
Balashov
S P
SP
Center for Biophysics and Computational Biology, Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, B107 CLSL, 601 S. Goodwin Ave., 61801, Urbana, IL, USA. sbalasho@uiuc.edu
D000596:Amino Acids / Q000737:chemistry; D001436:Bacteriorhodopsins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008027:Light; D008956:Models, Chemical; D010777:Photochemistry; D017494:Proton Pumps / Q000737:chemistry*; D012545:Schiff Bases / Q000737:chemistry
D000596:Amino Acids; D017494:Proton Pumps; D012545:Schiff Bases; D001436:Bacteriorhodopsins