Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway (Q27676244)

2

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Christopher S Lunde

3

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Shahab Rouhani

4

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Robert M Glaeser

5

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Yong Duan

6

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Marc T Facciotti

Directional proton transfer in membrane proteins achieved through protonated protein-bound water molecules: a proton diode

7

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publication date

5 February 2013

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published in

Structure

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volume

21

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issue

2

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page(s)

290-7

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cites work

1 reference

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Structure of an early intermediate in the M-state phase of the bacteriorhodopsin photocycle

20 March 2017

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Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

20 March 2017

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Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin

20 March 2017

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Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution

20 March 2017

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Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution

20 March 2017

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Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium

20 March 2017

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A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations

20 March 2017

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Proton transfer via a transient linear water-molecule chain in a membrane protein

7 April 2017

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Structural snapshots of conformational changes in a seven-helix membrane protein: lessons from bacteriorhodopsin

29 September 2017

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Structural changes in the N and N' states of the bacteriorhodopsin photocycle

29 September 2017

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The energetics of the primary proton transfer in bacteriorhodopsin revisited: it is a sequential light-induced charge separation after all

29 September 2017

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Structures and spectral signatures of protonated water networks in bacteriorhodopsin

29 September 2017

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Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy

29 September 2017

1 reference

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The barrier for proton transport in aquaporins as a challenge for electrostatic models: the role of protein relaxation in mutational calculations

29 September 2017

1 reference

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Water as a cofactor in the unidirectional light-driven proton transfer steps in bacteriorhodopsin

29 September 2017

1 reference

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Proton transfers in the bacteriorhodopsin photocycle

29 September 2017

1 reference

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Proton binding within a membrane protein by a protonated water cluster

29 September 2017

1 reference

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Water molecules and hydrogen-bonded networks in bacteriorhodopsin--molecular dynamics simulations of the ground state and the M-intermediate

29 September 2017

1 reference

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How environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation

29 September 2017

1 reference

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Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment

29 September 2017

1 reference

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What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals

29 September 2017

1 reference

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The role of small intraprotein cavities in the catalytic cycle of bacteriorhodopsin

29 September 2017

1 reference

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Subsecond proton-hole propagation in bacteriorhodopsin

29 September 2017

1 reference

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Time-resolved X-ray diffraction reveals movement of F helix of D96N bacteriorhodopsin during M-MN transition at neutral pH.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Time-resolved x-ray diffraction reveals multiple conformations in the M-N transition of the bacteriorhodopsin photocycle

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Proton transfer reactions across bacteriorhodopsin and along the membrane

29 September 2017

1 reference

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Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography

29 September 2017

1 reference

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Closing in on bacteriorhodopsin: progress in understanding the molecule

29 September 2017

1 reference

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In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy

29 September 2017

1 reference

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pH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopy

29 September 2017

1 reference

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Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analogues

29 September 2017

1 reference

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Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

A defective proton pump, point-mutated bacteriorhodopsin Asp96----Asn is fully reactivated by azide.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Role of aspartate-96 in proton translocation by bacteriorhodopsin.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Fourier transform infrared spectra of a late intermediate of the bacteriorhodopsin photocycle suggest transient protonation of Asp-212.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Acid-base equilibrium of the Schiff base in bacteriorhodopsin.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

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

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Active internal waters in the bacteriorhodopsin photocycle. A comparative study of the L and M intermediates at room and cryogenic temperatures by infrared spectroscopy.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Computational analysis of the proton translocation from Asp96 to schiff base in bacteriorhodopsin.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Membrane-protein stability in a phospholipid-based crystallization medium.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Water dynamics simulation as a tool for probing proton transfer pathways in a heptahelical membrane protein

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Proton Affinity Changes Driving Unidirectional Proton Transport in the Bacteriorhodopsin Photocycle

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Proton translocation by bacteriorhodopsin in the absence of substantial conformational changes.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of Asp-96 in the N photointermediate of bacteriorhodopsin

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3642035

Substitution of membrane-embedded aspartic acids in bacteriorhodopsin causes specific changes in different steps of the photochemical cycle

27 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23394942

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23394942

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23394942