(Q42173725)

English

Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides

scientific article published on February 2009

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides (English)

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

Rhodobacter sphaeroides

object named as

Rhodobacter sphaeroides

1 reference

based on heuristic

inferred from title

author name string

Tatsuya Iwata

1

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

Mark L Paddock

2

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

Melvin Y Okamura

3

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

Hideki Kandori

4

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

language of work or name

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publication date

1 February 2009

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

48

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

6

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

1220-1229

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

The assignment of the different infrared continuum absorbance changes observed in the 3000-1800-cm(-1) region during the bacteriorhodopsin photocycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Role of internal water molecules in bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Proton and electron transfer in bacterial reaction centers

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Proton uptake by carboxylic acid groups upon photoreduction of the secondary quinone (QB) in bacterial reaction centers from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Asymmetric binding of the 1- and 4-C=O groups of QA in Rhodobacter sphaeroides R26 reaction centres monitored by Fourier transform infra-red spectroscopy using site-specific isotopically labelled ubiquinone-10

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Pathway of proton transfer in bacterial reaction centers: replacement of serine-L223 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Probing the secondary quinone (QB) environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Proton transfer in reaction centers from photosynthetic bacteria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

26 October 2017

Proton and electron transfer in the acceptor quinone complex of Rhodobacter sphaeroides reaction centers: characterization of site-directed mutants of the two ionizable residues, GluL212 and AspL213, in the QB binding site

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

29 May 2018

An isotope-edited FTIR investigation of the role of Ser-L223 in binding quinone (QB) and semiquinone (QB-) in the reaction center from Rhodobacter sphaeroides

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Strongly hydrogen-bonded water molecules in the Schiff base region of rhodopsins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

FTIR studies of internal water molecules in the Schiff base region of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Identification of a novel protonation pattern for carboxylic acids upon Q(B) photoreduction in Rhodobacter sphaeroides reaction center mutants at Asp-L213 and Glu-L212 sites

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Vibrational spectroscopy favors a unique QB binding site at the proximal position in wild-type reaction centers and in the Pro-L209 --> Tyr mutant from Rhodobacter sphaeroides

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Vibrational frequency and dipolar orientation of the protonated Schiff base in bacteriorhodopsin before and after photoisomerization

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases proton uptake by Glu-L212 upon first electron transfer to QB in reaction centers from Rhodobacter sphaeroides

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Identification of the proton pathway in bacterial reaction centers: cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (QB).

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Pathway of proton transfer in bacterial reaction centers: role of aspartate-L213 in proton transfers associated with reduction of quinoneto dihydroquinone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

Pathway of proton transfer in bacterial reaction centers: further investigations on the role of Ser-L223 studied by site-directed mutagenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2701474

17 August 2018

The unusually strong hydrogen bond between the carbonyl of Q(A) and His M219 in the Rhodobacter sphaeroides reaction center is not essential for efficient electron transfer from Q(A)(-) to Q(B)

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Water Molecules in the Schiff Base Region of Bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Iron-depleted reaction centers from Rhodopseudomonas sphaeroides R-26.1: characterization and reconstitution with Fe2+, Mn2+, Co2+, Ni2+, Cu2+, and Zn2+

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Probing the primary quinone environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: assignment of the interactions of each carbonyl of QA in Rhodobacter sphaeroides using site-specific 13C-labeled ubiqu

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

FTIR spectroscopy shows weak symmetric hydrogen bonding of the QB carbonyl groups in Rhodobacter sphaeroides R26 reaction centres

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: symmetry of the carbonyl interactions and close equivalence of the QB vibrations in Rhodobacter sphaeroides and Rhodop

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Fourier Transform Infrared Difference Spectroscopy of Secondary Quinone Acceptor Photoreduction in Proton Transfer Mutants of Rhodobacter sphaeroides

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Electrostatic influence of QA reduction on the IR vibrational mode of the 10a-ester C==O of HA demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Hydrogen bonding interaction between the primary quinone acceptor QA and a histidine side chain in photosystem II as revealed by Fourier transform infrared spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Steady-state FTIR spectra of the photoreduction of QA and QB in Rhodobacter sphaeroides reaction centers provide evidence against the presence of a proposed transient electron acceptor X between the two quinones

1 reference

https://pubmed.ncbi.nlm.nih.gov/19161296

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI801990S

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 October 2017

ResearchGate publication ID

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