Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction. (Q37715168)

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16 October 2019

title

Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction (English)

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16 October 2019

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4

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16 October 2019

author name string

H Kamikubo

1

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16 October 2019

M Kataoka

2

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16 October 2019

G Váró

3

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16 October 2019

F Tokunaga

5

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16 October 2019

R Needleman

6

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16 October 2019

J K Lanyi

7

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16 October 2019

language of work or name

English

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publication date

1 February 1996

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Proceedings of the National Academy of Sciences of the United States of America

16 October 2019

published in

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16 October 2019

volume

93

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16 October 2019

issue

4

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16 October 2019

page(s)

1386-1390

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

16 October 2019

cites work

1 reference

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The bacteriorhodopsin photocycle: direct structural study of two substrates of the M-intermediate

23 August 2017

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Two progressive substrates of the M-intermediate can be identified in glucose-embedded, wild-type bacteriorhodopsin

23 August 2017

1 reference

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Bacteriorhodopsin as a model for proton pumps

23 August 2017

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Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumping

23 August 2017

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Simple Allosteric Model for Membrane Pumps

23 August 2017

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Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane

23 August 2017

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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

23 August 2017

1 reference

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Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction

23 August 2017

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

23 August 2017

1 reference

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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

23 August 2017

1 reference

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

23 August 2017

1 reference

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Protein changes associated with reprotonation of the Schiff base in the photocycle of Asp96-->Asn bacteriorhodopsin. The MN intermediate with unprotonated Schiff base but N-like protein structure

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.

23 August 2017

1 reference

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

28 September 2017

1 reference

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

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

Photoreaction of the N intermediate of bacteriorhodopsin, and its relationship to the decay kinetics of the M intermediate

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

Pathway of proton uptake in the bacteriorhodopsin photocycle

23 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

Chromophore structure in bacteriorhodopsin's N intermediate: implications for the proton-pumping mechanism

23 June 2018

1 reference

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Transient spectroscopy of bacterial rhodopsins with an optical multichannel analyzer. 1. Comparison of the photocycles of bacteriorhodopsin and halorhodopsin

23 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium

23 June 2018

1 reference

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Protonation and deprotonation of the M, N, and O intermediates during the bacteriorhodopsin photocycle.

23 June 2018

1 reference

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Thermodynamics and energy coupling in the bacteriorhodopsin photocycle

23 June 2018

1 reference

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Crystallographic characterization by X-ray diffraction of the M-intermediate from the photo-cycle of bacteriorhodopsin at room temperature

23 June 2018

1 reference

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

23 June 2018

1 reference

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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.

23 June 2018

1 reference

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Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle

23 June 2018

1 reference

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Bacteriorhodopsin reconstituted from two individual helices and the complementary five-helix fragment is photoactive

23 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

Pathways of the rise and decay of the M photointermediate(s) of bacteriorhodopsin

23 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=39947

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

1 September 2018

1 reference

12 December 2020

Fourier transform infrared study of the N intermediate of bacteriorhodopsin

1 reference

12 December 2020

Photoreaction of N560 intermediate in the photocycle of bacteriorhodopsin

1 reference

12 December 2020

Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change

1 reference

12 December 2020

Bacteriorhodopsin photoreaction: identification of a long-lived intermediate N (P,R350) at high pH and its M-like photoproduct

1 reference

12 December 2020

Asp96 deprotonation and transmembrane alpha-helical structural changes in bacteriorhodopsin

1 reference

12 December 2020

Energy coupling in an ion pump. The reprotonation switch of bacteriorhodopsin

1 reference

12 December 2020

Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR-->N transition

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.93.4.1386

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8643641%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

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16 October 2019

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