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Aspartate–Histidine Interaction in the Retinal Schiff Base Counterion of the Light-Driven Proton Pump of Exiguobacterium sibiricum

Biochemistry (Easton), 2012-07, Vol.51 (29), p.5748-5762

2012

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Crystal Structure of Sensory Rhodopsin II at 2.4 Angstroms: Insights into Color Tuning and Transducer Interaction

Science (American Association for the Advancement of Science), 2001-08, Vol.293 (5534), p.1499-1503

2001

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Structural Changes in Bacteriorhodopsin During Ion Transport at 2 Angstrom Resolution

Science (American Association for the Advancement of Science), 1999-10, Vol.286 (5438), p.255-260

1999

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Control of retinal isomerization in bacteriorhodopsin in the high-intensity regime

Proceedings of the National Academy of Sciences - PNAS, 2009-07, Vol.106 (27), p.10896-10900

2009

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Proton Transfer Pathways in Bacteriorhodopsin at 2.3 Angstrom Resolution

Science (American Association for the Advancement of Science), 1998-06, Vol.280 (5371), p.1934-1937

1998

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Xanthorhodopsin: Proton pump with a carotenoid antenna

Cellular and molecular life sciences : CMLS, 2007-09, Vol.64 (18), p.2323-2328

2007

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Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin

BBA - Bioenergetics, 1993-12, Vol.1183 (2), p.241-261

Lanyi, Janos K.

1993

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Molecular Mechanism of Spectral Tuning in Sensory Rhodopsin II

Biochemistry (Easton), 2001-11, Vol.40 (46), p.13906-13914

2001

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Bacteriorhodopsin as a model for proton pumps

Nature (London), 1995-06, Vol.375 (6531), p.461-463

Lanyi, Janos K

1995

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Progress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin

FEBS Letters, 1999-12, Vol.464 (3), p.103-107

Lanyi, Janos K

1999

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Protein Catalysis of the Retinal Subpicosecond Photoisomerization in the Primary Process of Bacteriorhodopsin Photosynthesis

Science (American Association for the Advancement of Science), 1993-08, Vol.261 (5123), p.891-894

1993

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Pathways of proton release in the bacteriorhodopsin photocycle

Biochemistry (Easton), 1992-09, Vol.31 (36), p.8535-8543

1992

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Coupling of the Reisomerization of the Retinal, Proton Uptake, and Reprotonation of Asp-96 in the N Photointermediate of Bacteriorhodopsin

Biochemistry (Easton), 2001-09, Vol.40 (38), p.11308-11317

2001

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Bacteriorhodopsin

Biochimica et biophysica acta, 2000-08, Vol.1460 (1), p.1-3

Lanyi, Janos K

2000

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Bacteriorhodopsin

Current Opinion in Structural Biology, 2001-08, Vol.11 (4), p.415-419

2001

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Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps

The Journal of biological chemistry, 1997-12, Vol.272 (50), p.31209-31212

Lanyi, J K

1997

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Proton Transfers in the Photochemical Reaction Cycle of Proteorhodopsin

Biochemistry (Easton), 2002-04, Vol.41 (17), p.5348-5358

2002

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ESR — A retinal protein with unusual properties from Exiguobacterium sibiricum

Biochemistry (Moscow), 2015-06, Vol.80 (6), p.688-700

2015

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Halorhodopsin, a light-driven electrogenic chloride-transport system

Physiological reviews, 1990-04, Vol.70 (2), p.319-330

LANYI, J. K

1990

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Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base

Biochemistry (Easton), 1991-11, Vol.30 (45), p.10972-10979

1991

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X-ray crystallography of bacteriorhodopsin and its photointermediates: insights into the mechanism of proton transport

Biochemistry (Moscow), 2001-11, Vol.66 (11), p.1192-1196

Lanyi, J K

2001

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Structure of the N Intermediate of Bacteriorhodopsin Revealed by X-Ray Diffraction

Proceedings of the National Academy of Sciences - PNAS, 1996-02, Vol.93 (4), p.1386-1390

1996

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Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle

Biophysical journal, 1993-07, Vol.65 (1), p.124-130

1993

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Properties of Asp212----Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base

The Journal of biological chemistry, 1991-06, Vol.266 (18), p.11478-11484

1991

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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

Biochemistry (Easton), 1994-02, Vol.33 (7), p.1713-1717

1994

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Aspartate–Histidine Interaction in the Retinal Schiff Base Counterion of the Light-Driven Proton Pump of Exiguobacterium sibiricum

Crystal Structure of Sensory Rhodopsin II at 2.4 Angstroms: Insights into Color Tuning and Transducer Interaction

Structural Changes in Bacteriorhodopsin During Ion Transport at 2 Angstrom Resolution

Control of retinal isomerization in bacteriorhodopsin in the high-intensity regime

Proton Transfer Pathways in Bacteriorhodopsin at 2.3 Angstrom Resolution

Xanthorhodopsin: Proton pump with a carotenoid antenna

Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin

Molecular Mechanism of Spectral Tuning in Sensory Rhodopsin II

Bacteriorhodopsin as a model for proton pumps

Progress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin

Protein Catalysis of the Retinal Subpicosecond Photoisomerization in the Primary Process of Bacteriorhodopsin Photosynthesis

Pathways of proton release in the bacteriorhodopsin photocycle

Coupling of the Reisomerization of the Retinal, Proton Uptake, and Reprotonation of Asp-96 in the N Photointermediate of Bacteriorhodopsin

Bacteriorhodopsin

Bacteriorhodopsin

Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps

Proton Transfers in the Photochemical Reaction Cycle of Proteorhodopsin

ESR — A retinal protein with unusual properties from Exiguobacterium sibiricum

Halorhodopsin, a light-driven electrogenic chloride-transport system

Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base

X-ray crystallography of bacteriorhodopsin and its photointermediates: insights into the mechanism of proton transport

Structure of the N Intermediate of Bacteriorhodopsin Revealed by X-Ray Diffraction

Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle

Properties of Asp212----Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base

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

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