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Literature summary for 7.1.1.4 extracted from
- Structure and coordination of CuB in the Acidianus ambivalens aa3 quinol oxidase heme-copper center (2005), J. Biol. Inorg. Chem., 10, 625-635.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| copper | a type B heme-copper oxygen reductase. The binuclear Fea3Cu(B) center is the site of dioxygen chemistry and is involved in the proton translocation mechanism. The catalytic bimetallic Cu(B) center is probed in a number of different states using extended X-ray absorption fine structure (EXAFS) spectroscopy. The oxidized CuB center is four-coordinated with three histidine residues and one oxygen atom. No significant change in the protein structure in the vicinity of Cu(B) is observed upon reduction, apart from the release of the oxo ligand | Acidianus ambivalens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidianus ambivalens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Acidianus ambivalens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aa3 quinol oxidase | - |
Acidianus ambivalens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | a type B heme-copper oxygen reductase | Acidianus ambivalens | |
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