(Q30832019)

English

Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

1 reference

based on heuristic

inferred from title

Rhodobacter sphaeroides

object named as

Rhodobacter sphaeroides

1 reference

based on heuristic

inferred from title

Dieter Oesterhelt

5

object named as

Dieter Oesterhelt

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

author name string

Francesco Francia

1

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Jun Wang

2

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Hans Zischka

3

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Giovanni Venturoli

4

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

language of work or name

0 references

publication date

1 April 2002

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

269

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

7

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

1877-1885

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Proton and electron transfer in bacterial reaction centers

1 reference

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21 January 2018

The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum

1 reference

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21 January 2018

Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria

1 reference

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Mutation of the Ser2 codon of the light-harvesting B870 alpha polypeptide of Rhodobacter capsulatus partially suppresses the pufX phenotype

1 reference

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21 January 2018

Consequences for the organization of reaction center-light harvesting antenna 1 (LH1) core complexes of Rhodobacter sphaeroides arising from deletion of amino acid residues from the C terminus of the LH1 alpha polypeptide.

1 reference

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21 January 2018

Supramolecular complexes in photosynthetic bacteria

1 reference

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21 January 2018

Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides

1 reference

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21 January 2018

The long-range supraorganization of the bacterial photosynthetic unit: A key role for PufX.

1 reference

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21 January 2018

Isolation of the PufX protein from Rhodobacter capsulatus and Rhodobacter sphaeroides: evidence for its interaction with the alpha-polypeptide of the core light-harvesting complex

1 reference

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21 January 2018

Secondary electron transfer in chromatophores of Rhodopseudomonas capsulata A1a pho. Binary out-of-phase oscillations in ubisemiauinone formation and cytochrome b50 reduction with consective light flashes

1 reference

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21 January 2018

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

1 reference

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21 January 2018

Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins

1 reference

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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

1 reference

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Demonstration of a collisional interaction of ubiquinol with the ubiquinol-cytochrome c2 oxidoreductase complex in chromatophores from Rhodobacter sphaeroides.

1 reference

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Global analysis of biochemical and biophysical data

1 reference

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THE ROLE OF THE QUINONE POOL IN THE CYCLIC ELECTRON-TRANSFER CHAIN OF RHODOPSEUDOMONAS SPHAEROIDES: A MODIFIED Q-CYCLE MECHANISM

1 reference

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21 January 2018

Ubiquinone in Rhodopseudomonas sphaeroides. Some thermodynamic properties

1 reference

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Transmembrane helices predicted at 95% accuracy

1 reference

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Role of the core region of the PufX protein in inhibition of reconstitution of the core light-harvesting complexes of Rhodobacter sphaeroides and Rhodobacter capsulatus

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1033.2002.02834.X

21 January 2018

Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria

1 reference

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21 January 2018

Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone/ubiquinol exchange between the reaction center QB site and the cytochrome bc1 complex

1 reference

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21 January 2018

The Reaction Center−LH1 Antenna Complex ofRhodobactersphaeroidesContains One PufX Molecule Which Is Involved in Dimerization of This Complex

1 reference

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21 January 2018

Reconstitution of cyclic electron transport and photophosphorylation by incorporation of the reaction center, cytochrome bc1 complex and ATP synthase from Rhodobacter capsulatus into ubiquinone-10/phospholipid vesicles

1 reference

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21 January 2018

Structure and function of bacterial photosynthetic reaction centres

1 reference

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Pleiotropic effects of pufX gene deletion on the structure and function of the photosynthetic apparatus of Rhodobacter capsulatus

1 reference

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21 January 2018

Photosynthetic deficiency of a pufX deletion mutant of Rhodobacter sphaeroides is suppressed by point mutations in the light-harvesting complex genes pufB or pufA

1 reference

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21 January 2018

The Rhodobacter sphaeroides PufX protein is not required for photosynthetic competence in the absence of a light harvesting system

1 reference

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21 January 2018

The LH1-RC core complex of Rhodobacter sphaeroides: interaction between components, time-dependent assembly, and topology of the PufX protein

1 reference

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21 January 2018

Identifiers

10.1046/J.1432-1033.2002.02834.X

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

ResearchGate publication ID

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