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142 related items for PubMed ID: 2040618

  • 1. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M----N transition.
    Bousché O, Braiman M, He YW, Marti T, Khorana HG, Rothschild KJ.
    J Biol Chem; 1991 Jun 15; 266(17):11063-7. PubMed ID: 2040618
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  • 2. A redirected proton pathway in the bacteriorhodopsin mutant Tyr-57-->Asp. Evidence for proton translocation without Schiff base deprotonation.
    Sonar S, Marti T, Rath P, Fischer W, Coleman M, Nilsson A, Khorana HG, Rothschild KJ.
    J Biol Chem; 1994 Nov 18; 269(46):28851-8. PubMed ID: 7961844
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  • 3. Time-resolved Fourier transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay.
    Bousché O, Sonar S, Krebs MP, Khorana HG, Rothschild KJ.
    Photochem Photobiol; 1992 Dec 18; 56(6):1085-95. PubMed ID: 1337213
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  • 4. 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
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  • 7. A linkage of the pKa's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin.
    Richter HT, Brown LS, Needleman R, Lanyi JK.
    Biochemistry; 1996 Apr 02; 35(13):4054-62. PubMed ID: 8672439
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  • 8. 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
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  • 9. 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.
    Otto H, Marti T, Holz M, Mogi T, Stern LJ, Engel F, Khorana HG, Heyn MP.
    Proc Natl Acad Sci U S A; 1990 Feb 25; 87(3):1018-22. PubMed ID: 2153966
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  • 11. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212.
    Braiman MS, Mogi T, Marti T, Stern LJ, Khorana HG, Rothschild KJ.
    Biochemistry; 1988 Nov 15; 27(23):8516-20. PubMed ID: 2851326
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  • 12. Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change.
    Cao Y, Váró G, Klinger AL, Czajkowsky DM, Braiman MS, Needleman R, Lanyi JK.
    Biochemistry; 1993 Mar 02; 32(8):1981-90. PubMed ID: 8448157
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  • 14. Fourier transform infrared spectra of a late intermediate of the bacteriorhodopsin photocycle suggest transient protonation of Asp-212.
    Dioumaev AK, Brown LS, Needleman R, Lanyi JK.
    Biochemistry; 1999 Aug 03; 38(31):10070-8. PubMed ID: 10433714
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  • 17. Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopy.
    Maeda A, Sasaki J, Shichida Y, Yoshizawa T, Chang M, Ni B, Needleman R, Lanyi JK.
    Biochemistry; 1992 May 19; 31(19):4684-90. PubMed ID: 1316157
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  • 18. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds.
    Rothschild KJ, He YW, Sonar S, Marti T, Khorana HG.
    J Biol Chem; 1992 Jan 25; 267(3):1615-22. PubMed ID: 1730706
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