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Literature summary for 7.1.1.5 extracted from
- Heme biosynthesis is coupled to electron transport chains for energy generation (2010), Proc. Natl. Acad. Sci. USA, 107, 10436-10441.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Cyd oxidase | - |
Escherichia coli |
| cytochrome bd oxidase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cyo, Cyd and Nar contribute to the proton motive force that drives ATP formation. oxygen-dependent cytochrome oxidases, cytochrome bo3 (Cyo) and cytochrome bd (Cyd) oxidase, sustain up to 67% (Cyd) and 78% (Cyo) of HemG activity in the absence of ubiquinone, indicating a tight association of the quinones with the enzyme complexes during preparation | Escherichia coli |
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Release 2023.1 (January 2023)
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