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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
7.1.1.6 | chloroplast | - |
Chlamydomonas reinhardtii | 9507 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.1.1.6 | Chlamydomonas reinhardtii | P23577 | subunit PetA | - |
7.1.1.6 | Mastigocladus laminosus | P83791 | subunit PetB | - |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
7.1.1.6 | cytochrome b6f | - |
Mastigocladus laminosus |
7.1.1.6 | PetA | - |
Chlamydomonas reinhardtii |
7.1.1.6 | PetB | - |
Mastigocladus laminosus |