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Literature summary extracted from

  • Ustynyuk, L.; Tikhonov, A.
    The cytochrome b6f complex DFT modeling of the first step of plastoquinol oxidation by the iron-sulfur protein (2018), J. Organomet. Chem., 867, 290-299 .
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.1.1.6 modeling of the first step of plastoquinol PQH2 oxidation by the iron-sulfur protein of the Cyt b6f complex. The H-transfer reaction displays a bidirectional mechanism, an electron is directed to the Fe(1) atom of the [Fe2S2] cluster of the iron-sulfur protein, and a proton is accepted by the Nepsilon atom of the His155 residue liganding the Fe(1) atom. Results support a diabatic model of the H-transfer, which implies that the elementary steps of electron and proton transfer occur much more rapidly than the concomitant changes in the system geometry Mastigocladus laminosus
7.1.1.6 modeling of the first step of plastoquinol PQH2 oxidation by the iron-sulfur protein of the Cyt b6f complex. The H-transfer reaction displays a bidirectional mechanism, an electron is directed to the Fe(1) atom of the [Fe2S2] cluster of the iron-sulfur protein, and a proton is accepted by the Nepsilon atom of the His155 residue liganding the Fe(1) atom. Results support a diabatic model of the H-transfer, which implies that the elementary steps of electron and proton transfer occur much more rapidly than the concomitant changes in the system geometry Chlamydomonas reinhardtii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.6 chloroplast
-
Chlamydomonas reinhardtii 9507
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Organism

EC Number Organism UniProt Comment Textmining
7.1.1.6 Chlamydomonas reinhardtii P23577 subunit PetA
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7.1.1.6 Mastigocladus laminosus P83791 subunit PetB
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Synonyms

EC Number Synonyms Comment Organism
7.1.1.6 cytochrome b6f
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Mastigocladus laminosus
7.1.1.6 PetA
-
Chlamydomonas reinhardtii
7.1.1.6 PetB
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Mastigocladus laminosus