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Literature summary for 7.1.1.6 extracted from

  • Hasan, S.S.; Yamashita, E.; Baniulis, D.; Cramer, W.A.
    Quinone-dependent proton transfer pathways in the photosynthetic cytochrome b6f complex (2013), Proc. Natl. Acad. Sci. USA, 110, 4297-4302.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
free enzyme and enzyme complexed with with quinone analogue inhibitors tridecyl-stigmatellin and 2-nonyl-4-hydroxyquinoline N-oxide, X-ray diffraction structure determination at 2.70 A, 3.07 A, and 3.25 A resolution, respectively Mastigocladus laminosus

Inhibitors

Inhibitors Comment Organism Structure
2-nonyl-4-hydroxyquinoline N-oxide
-
 Mastigocladus laminosus
tridecyl-stigmatellin
-
 Mastigocladus laminosus

Organism

Organism UniProt Comment Textmining
Mastigocladus laminosus
-
-
-

Synonyms

Synonyms Comment Organism
photosynthetic cytochrome b6f complex
-
 Mastigocladus laminosus

General Information

General Information Comment Organism
additional information proton uptake pathway from the electrochemically negative (n) aqueous phase to the n-side quinone binding site of the complex, and a probable route for proton exit to the positive phase resulting from quinol oxidation, overview. The simplest n-side proton pathway extends from the aqueous phase via Asp20 and Arg207 (cytochrome b6 subunit) to quinone bound axially to heme cn. On the positive side, the heme-proximal Glu78 (subunit IV), which accepts protons from plastosemiquinone, defines a route for H+ transfer to the aqueous phase Mastigocladus laminosus
physiological function two-thirds of the proton gradient used for transmembrane free energy storage in oxygenic photosynthesis is generated by the cytochrome b6f complex Mastigocladus laminosus