STRUCTURE-FUNCTION STUDIES ON BACTERIORHODOPSIN .10. INDIVIDUAL SUBSTITUTIONS OF ARGININE RESIDUES BY GLUTAMINE AFFECT CHROMOPHORE FORMATION, PHOTOCYCLE, AND PROTON TRANSLOCATION
- 25 August 1989
- journal article
- research article
- Vol. 264 (24) , 14202-14208
Abstract
We have individually replaced all 7 of the arginine residues in bacteriorhodopsin by glutamine. The mutants with substitutions at positions 7, 164, 175, and 225 showed essentially the wild-type phenotype in regard to chromophore regeneration, chromophore .lambda.max, and proton pumping, although the mutant Arg-175 .fwdarw. Gln showed decreased rate of chromophore regeneration. Glutamine substitutions of Arg-82, -134, and -227 affected proton pumping ability, and caused specific alterations in the bacteriorhodopsin photocycle. Finally, electrostatic interactions are proposed between Arg-82 and -227, and specific carboxylic acid residues in helices C and G, which regulate the purple to blue transition and proton transfers during the photocycle.This publication has 5 references indexed in Scilit:
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