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Literature summary for 7.1.1.6 extracted from

  • Hasan, S.S.; Stofleth, J.T.; Yamashita, E.; Cramer, W.A.
    Lipid-induced conformational changes within the cytochrome b6f complex of oxygenic photosynthesis (2013), Biochemistry, 52, 2649-2654.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.1.6

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffuion method, 0.0015 ml protein solution, containing 0.135-0.18 mM protein, is mixed with 0.0015 ml of reservoir solution, containing 100 mM Tris-HCl, pH 8.5, 200 mM MgCl2, 40 mM CdCl2, and 16?17% PEG-550 monomethyl ether, 4 °C, hexagonal bipyramidal crystals appear in 24?36 h, X-ray diffraction structure determination at 2.8 A resolution Mastigocladus laminosus

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid membrane
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 Mastigocladus laminosus 42651
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Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ Rieske iron-sulfur protein, ISP, containing a [2Fe-2S] cluster, conformational flexibility of the cyt b6 f ISP subunit Mastigocladus laminosus

Organism

Organism UniProt Comment Textmining
Mastigocladus laminosus P83791
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Purification (Commentary)

Purification (Comment) Organism
partial purification from thylakoid membranes by ammonium sulfate precipitation and hydrophobic interaction chromatography Mastigocladus laminosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information detectable conformational changes in the ISP binding site of cyt b6 f in presence of dioleoylphosphatidylglycerol and dioleoylphosphatidylcholine Mastigocladus laminosus ?
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 ?

Synonyms

Synonyms Comment Organism
Cyt b6 f
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 Mastigocladus laminosus
cytochrome b6 f
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 Mastigocladus laminosus
cytochrome b6 f complex
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 Mastigocladus laminosus

General Information

General Information Comment Organism
physiological function cytochrome b6 f catalyzes quinone redox reactions within photosynthetic membranes to generate a transmembrane proton electrochemical gradient for ATP synthesis. A key step involves the transfer of an electron from the [2Fe-2S] cluster of the iron-sulfur protein extrinsic domain to the cytochrome f heme across a distance of 26 A, which is too large for competent electron transfer but could be bridged by translation-rotation of the iron-sulfur protein Mastigocladus laminosus