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Literature summary for 1.8.98.1 extracted from
- A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from Methanothermobacter marburgensis (2007), Biochemistry, 46, 12875-12885.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| subunit HdrB is produced in Escherichia coli | Methanothermobacter marburgensis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | the C-terminal CCG domain of the subunit B of heterodisulfide binds to the [4Fe-4S]3+ cluster | Methanothermobacter marburgensis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanothermobacter marburgensis | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| heterodisulfide reductase | - |
Methanothermobacter marburgensis |
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Release 2023.1 (January 2023)
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