Crystallization (Comment) | Organism |
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X-ray diffraction structure determination at 3.0 A resolution and analysis, modeling, overview | Thermosynechococcus vestitus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Thermosynechococcus vestitus | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermosynechococcus vestitus | Q8DKZ3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Thermosynechococcus vestitus | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? |
Synonyms | Comment | Organism |
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photosynthetic complex I | - |
Thermosynechococcus vestitus |
General Information | Comment | Organism |
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additional information | X-ray diffraction structure determination at 3.0 A resolution and analysis, modeling, and structure-function analysis, overview. The model reveals structural adaptations that facilitate binding and electron transfer from the photosynthetic electron carrier ferredoxin. Ferredoxin directly mediates electron transfer between photosystem I and complex I, instead of using intermediates such as NADPH (the reduced form of nicotinamide adenine dinucleotide phosphate). A large rate constant for association of ferredoxin to complex I indicates efficient recognition, with the protein subunit NdhS being the key component in this process | Thermosynechococcus vestitus |
physiological function | photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion | Thermosynechococcus vestitus |