The residues Leu 93 and Asp 96 act independently in the bacteriorhodopsin photocycle: studies with the leu 93-->Ala, Asp 96-->Asn double mutant
Open Access
- 1 May 1996
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 70 (5) , 2366-2372
- https://doi.org/10.1016/s0006-3495(96)79803-x
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- The Proton Transfers in the Cytoplasmic Domain of Bacteriorhodopsin are Facilitated by a Cluster of Interacting ResiduesJournal of Molecular Biology, 1994
- Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1993
- Mechanism of light-dependent proton translocation by bacteriorhodopsinJournal of Bacteriology, 1993
- Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization.Proceedings of the National Academy of Sciences, 1991
- Correlation between absorption maxima and thermal isomerization rates in bacteriorhodopsinBiophysical Journal, 1991
- The role of back-reactions and proton uptake during the N .fwdarw. O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman studyBiochemistry, 1990
- Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopyJournal of Molecular Biology, 1990
- Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.Proceedings of the National Academy of Sciences, 1990
- Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.Proceedings of the National Academy of Sciences, 1989
- Bacteriorhodopsin: a light-driven proton pump in Halobacterium HalobiumBiophysical Journal, 1975