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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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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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Bacteriorhodopsin

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

Lanyi, Janos K

2000

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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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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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Proton transfer and energy coupling in the bacteriorhodopsin photocycle

Journal of bioenergetics and biomembranes, 1992-04, Vol.24 (2), p.169-179

Lanyi, J. K.

1992

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Distortions in the photocycle of bacteriorhodopsin at moderate dehydration

Biophysical journal, 1991-02, Vol.59 (2), p.313-322

1991

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Local−Global Conformational Coupling in a Heptahelical Membrane Protein: Transport Mechanism from Crystal Structures of the Nine States in the Bacteriorhodopsin Photocycle

Biochemistry (Easton), 2004-01, Vol.43 (1), p.3-8

2004

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Proton pumps: mechanism of action and applications

Trends in Biotechnology, 2001-04, Vol.19 (4), p.140-144

2001

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Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopy

Biochemistry (Easton), 1992-05, Vol.31 (19), p.4684-4690

1992

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Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle

Biophysical journal, 1995-04, Vol.68 (4), p.1518-1530

1995

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Crystal structure of the D85S mutant of bacteriorhodopsin: model of an O-like photocycle intermediate

Journal of molecular biology, 2001-10, Vol.313 (3), p.615-628

2001

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Pathway of proton uptake in the bacteriorhodopsin photocycle

Biochemistry (Easton), 1993-08, Vol.32 (30), p.7669-7678

1993

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Intramembrane Signaling Mediated by Hydrogen-Bonding of Water and Carboxyl Groups in Bacteriorhodopsin and Rhodopsin

Journal of biochemistry (Tokyo), 1997-03, Vol.121 (3), p.399-406

1997

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Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle

Biophysical journal, 1995-11, Vol.69 (5), p.2103-2111

1995

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Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin ()

The Journal of biological chemistry, 1995-11, Vol.270 (45), p.27122-27126

1995

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

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

Bacteriorhodopsin

Proton Transfers in the Photochemical Reaction Cycle of Proteorhodopsin

ESR — A retinal protein with unusual properties from Exiguobacterium sibiricum

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

Proton transfer and energy coupling in the bacteriorhodopsin photocycle

Distortions in the photocycle of bacteriorhodopsin at moderate dehydration

Local−Global Conformational Coupling in a Heptahelical Membrane Protein: Transport Mechanism from Crystal Structures of the Nine States in the Bacteriorhodopsin Photocycle

Proton pumps: mechanism of action and applications

Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopy

Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle

Crystal structure of the D85S mutant of bacteriorhodopsin: model of an O-like photocycle intermediate

Pathway of proton uptake in the bacteriorhodopsin photocycle

Intramembrane Signaling Mediated by Hydrogen-Bonding of Water and Carboxyl Groups in Bacteriorhodopsin and Rhodopsin

Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle

Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin ()

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