(Q63442102)

English

Photooxidation of high-potential (c 559 , c 556 ) and low-potential (c 552 ) hemes in the cytochrome subunit of Rhodopseudomonas viridis reaction center

scientific article published on 01 November 1991

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scholarly article

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23 September 2019

Photooxidation of high-potential (c559, c556) and low-potential (c552) hemes in the cytochrome subunit of Rhodopseudomonas viridis reaction center. Characterization by FTIR spectroscopy (English)

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23 September 2019

Rhodopseudomonas viridis

object named as

Rhodopseudomonas viridis

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inferred from title

Catherine Berthomieu

2

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23 September 2019

author name string

Nabedryk E

1

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23 September 2019

Verméglio A

3

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23 September 2019

Breton J

4

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publication date

1 November 1991

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23 September 2019

293

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23 September 2019

1-2

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23 September 2019

53-58

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23 September 2019

Kinetics of oxidation of the bound cytochromes in reaction centers from Rhodopseudomonas viridis

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Electrogenic steps in the redox reactions catalyzed by photosynthetic reaction-centre complex from Rhodopseudomonas viridis

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

The acceptor quinone complex of Rhodopseudomonas viridis reaction centers

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Role of aspartate-96 in proton translocation by bacteriorhodopsin.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 A and comparison with the ferrocytochrome structure

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

High-resolution three-dimensional structure of horse heart cytochrome c

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Resonance Raman scattering from hemoproteins. Effects of ligands upon the Raman spectra of various C-type cytochromes

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

The pH dependence of the resonance Raman spectra and structural alterations at heme moieties of various cytochromes

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

A denaturation-induced proton-uptake study of horse ferricytochrome c.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

The structure, function and evolution of cytochromes

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981151-W

21 January 2018

Identifiers

10.1016/0014-5793(91)81151-W

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23 September 2019

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23 September 2019

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