Functional interactions in bacteriorhodopsin: a theoretical analysis of retinal hydrogen bonding with water (Q39649564)

13 September 2017

Functional interactions in bacteriorhodopsin: a theoretical analysis of retinal hydrogen bonding with water (English)

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13 September 2017

Nina M

1

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13 September 2017

Roux B

series ordinal

2

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13 September 2017

Smith JC

series ordinal

3

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13 September 2017

language of work or name

English

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publication date

1 January 1995

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13 September 2017

15

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inferred from page(s)

published in

Biophysical Journal

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13 September 2017

68

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13 September 2017

1

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13 September 2017

25-39

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Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy

13 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Molecular dynamics study of the proton pump cycle of bacteriorhodopsin

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Environmental effects on the protonation states of active site residues in bacteriorhodopsin

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Dark-adapted bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal Schiff bases

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Rhodopsin-like protein from the purple membrane of Halobacterium halobium

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Functions of a New Photoreceptor Membrane

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

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

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

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

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

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

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Proton polarizability of hydrogen bonds: infrared methods, relevance to electrochemical and biological systems

25 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

A molecular dynamics study of thermodynamic and structural aspects of the hydration of cavities in proteins.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

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

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Photochemistry and dark equilibrium of retinal isomers and bacteriorhodopsin isomers

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Identification of retinal isomers isolated from bacteriorhodopsin

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Hydrogen bonding interactions with the Schiff base of bacteriorhodopsin. Resonance Raman spectroscopy of the mutants D85N and D85A.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Solid-state 13C NMR studies of retinal in bacteriorhodopsin

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281657

Distorted structure of the retinal chromophore in bacteriorhodopsin resolved by 2H-NMR

4 November 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

Molecular dynamics study of bacteriorhodopsin and artificial pigments

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

Relative ground and excited state energies of CH3(CH = CH)5CH = NC4H9, its hydrogen-bonded and proton-transferred species, and charge partitioning and distribution in the protonated Schiff base of retinal

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M----N transition

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

Fourier transform infrared study of the N intermediate of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

The site of attachment of retinal in bacteriorhodopsin. A resonance Raman study

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

Solid-state 13C NMR of the retinal chromophore in photointermediates of bacteriorhodopsin: characterization of two forms of M

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711248

12 December 2020

10.1016/S0006-3495(95)80184-0

Identifiers

DOI

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13 September 2017

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13 September 2017

PubMed publication ID

7711248

1 reference