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4. Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement. Holz M, Drachev LA, Mogi T, Otto H, Kaulen AD, Heyn MP, Skulachev VP, Khorana HG. Proc Natl Acad Sci U S A; 1989 Apr; 86(7):2167-71. PubMed ID: 2648392 [Abstract] [Full Text] [Related]
7. Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation. Marti T, Otto H, Mogi T, Rösselet SJ, Heyn MP, Khorana HG. J Biol Chem; 1991 Apr 15; 266(11):6919-27. PubMed ID: 1849896 [Abstract] [Full Text] [Related]
8. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Otto H, Marti T, Holz M, Mogi T, Lindau M, Khorana HG, Heyn MP. Proc Natl Acad Sci U S A; 1989 Dec 15; 86(23):9228-32. PubMed ID: 2556706 [Abstract] [Full Text] [Related]
9. Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin. Marinetti T, Subramaniam S, Mogi T, Marti T, Khorana HG. Proc Natl Acad Sci U S A; 1989 Jan 15; 86(2):529-33. PubMed ID: 2536166 [Abstract] [Full Text] [Related]
13. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pump mechanism. Rothschild KJ, Braiman MS, He YW, Marti T, Khorana HG. J Biol Chem; 1990 Oct 05; 265(28):16985-91. PubMed ID: 2211604 [Abstract] [Full Text] [Related]
14. Light activates the reaction of bacteriorhodopsin aspartic acid-115 with dicyclohexylcarbodiimide. Renthal R, Cothran M, Espinoza B, Wall KA, Bernard M. Biochemistry; 1985 Jul 30; 24(16):4275-9. PubMed ID: 3931674 [Abstract] [Full Text] [Related]
18. Anion binding to the Schiff base of the bacteriorhodopsin mutants Asp-85----Asn/Asp-212----Asn and Arg-82----Gln/Asp-85----Asn/Asp-212----Asn. Marti T, Otto H, Rösselet SJ, Heyn MP, Khorana HG. J Biol Chem; 1992 Aug 25; 267(24):16922-7. PubMed ID: 1512233 [Abstract] [Full Text] [Related]