200 related articles for article (PubMed ID: 1646807)
1. Properties of Asp212----Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base.
Needleman R; Chang M; Ni B; Váró G; Fornés J; White SH; Lanyi JK
J Biol Chem; 1991 Jun; 266(18):11478-84. PubMed ID: 1646807
[TBL] [Abstract][Full Text] [Related]
2. Intramolecular charge transfer in the bacteriorhodopsin mutants Asp85-->Asn and Asp212-->Asn: effects of pH and anions.
Moltke S; Krebs MP; Mollaaghababa R; Khorana HG; Heyn MP
Biophys J; 1995 Nov; 69(5):2074-83. PubMed ID: 8580351
[TBL] [Abstract][Full Text] [Related]
3. Halide binding by the D212N mutant of Bacteriorhodopsin affects hydrogen bonding of water in the active site.
Shibata M; Yoshitsugu M; Mizuide N; Ihara K; Kandori H
Biochemistry; 2007 Jun; 46(25):7525-35. PubMed ID: 17547422
[TBL] [Abstract][Full Text] [Related]
4. Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model.
Brown LS; Dioumaev AK; Needleman R; Lanyi JK
Biophys J; 1998 Sep; 75(3):1455-65. PubMed ID: 9726947
[TBL] [Abstract][Full Text] [Related]
5. 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; 87(3):1018-22. PubMed ID: 2153966
[TBL] [Abstract][Full Text] [Related]
6. Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore.
Lanyi JK; Tittor J; Váró G; Krippahl G; Oesterhelt D
Biochim Biophys Acta; 1992 Jan; 1099(1):102-10. PubMed ID: 1346749
[TBL] [Abstract][Full Text] [Related]
7. The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.
Balashov SP; Govindjee R; Imasheva ES; Misra S; Ebrey TG; Feng Y; Crouch RK; Menick DR
Biochemistry; 1995 Jul; 34(27):8820-34. PubMed ID: 7612623
[TBL] [Abstract][Full Text] [Related]
8. The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.
Brown LS; Gat Y; Sheves M; Yamazaki Y; Maeda A; Needleman R; Lanyi JK
Biochemistry; 1994 Oct; 33(40):12001-11. PubMed ID: 7918419
[TBL] [Abstract][Full Text] [Related]
9. A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin.
Morgan JE; Gennis RB; Maeda A
Photochem Photobiol; 2008; 84(4):1038-45. PubMed ID: 18557823
[TBL] [Abstract][Full Text] [Related]
10. Time-resolved titrations of the Schiff base and of the Asp85 residue in artificial bacteriorhodopsins.
Druckmann S; Ottolenghi M; Rousso I; Friedman N; Sheves M
Biochemistry; 1995 Sep; 34(37):12066-74. PubMed ID: 7547945
[TBL] [Abstract][Full Text] [Related]
11. Hydration switch model for the proton transfer in the Schiff base region of bacteriorhodopsin.
Kandori H
Biochim Biophys Acta; 2004 Jul; 1658(1-2):72-9. PubMed ID: 15282177
[TBL] [Abstract][Full Text] [Related]
12. Aspartic acid 85 in bacteriorhodopsin functions both as proton acceptor and negative counterion to the Schiff base.
Subramaniam S; Greenhalgh DA; Khorana HG
J Biol Chem; 1992 Dec; 267(36):25730-3. PubMed ID: 1464589
[TBL] [Abstract][Full Text] [Related]
13. Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study.
Maeda A; Sasaki J; Yamazaki Y; Needleman R; Lanyi JK
Biochemistry; 1994 Feb; 33(7):1713-7. PubMed ID: 8110773
[TBL] [Abstract][Full Text] [Related]
14. FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor.
Bergo V; Spudich EN; Scott KL; Spudich JL; Rothschild KJ
Biochemistry; 2000 Mar; 39(11):2823-30. PubMed ID: 10715101
[TBL] [Abstract][Full Text] [Related]
15. Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state.
Dickopf S; Alexiev U; Krebs MP; Otto H; Mollaaghababa R; Khorana HG; Heyn MP
Proc Natl Acad Sci U S A; 1995 Dec; 92(25):11519-23. PubMed ID: 8524795
[TBL] [Abstract][Full Text] [Related]
16. Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation.
Metz G; Siebert F; Engelhard M
FEBS Lett; 1992 Jun; 303(2-3):237-41. PubMed ID: 1318849
[TBL] [Abstract][Full Text] [Related]
17. Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsin.
Imasheva ES; Balashov SP; Ebrey TG; Chen N; Crouch RK; Menick DR
Biophys J; 1999 Nov; 77(5):2750-63. PubMed ID: 10545374
[TBL] [Abstract][Full Text] [Related]
18. The Schiff base counterion of bacteriorhodopsin is protonated in sensory rhodopsin I: spectroscopic and functional characterization of the mutated proteins D76N and D76A.
Rath P; Olson KD; Spudich JL; Rothschild KJ
Biochemistry; 1994 May; 33(18):5600-6. PubMed ID: 8180184
[TBL] [Abstract][Full Text] [Related]
19. Hydrogen bonding interactions with the Schiff base of bacteriorhodopsin. Resonance Raman spectroscopy of the mutants D85N and D85A.
Rath P; Marti T; Sonar S; Khorana HG; Rothschild KJ
J Biol Chem; 1993 Aug; 268(24):17742-9. PubMed ID: 8349659
[TBL] [Abstract][Full Text] [Related]
20. Water molecules in the schiff base region of bacteriorhodopsin.
Shibata M; Tanimoto T; Kandori H
J Am Chem Soc; 2003 Nov; 125(44):13312-3. PubMed ID: 14582999
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]