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Literature summary for 1.14.14.18 extracted from
- The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism (2009), Biochemistry, 48, 3127-3137.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D140A | abolished activity, retains the unusual wild-type azide complex spin/orbital ground state | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | a pattern of substrate methyl contact shifts that places the lone iron pi-spin in the dxz orbital, rather than the dyz orbital found in the cyanide complex. Low-spin, (dxy)2(dyz,dxz)3, ground state in both azide and cyanide complexes. Switch from singly occupied dyz for the cyanide to dxz for the azide complex of HO is consistent with the orbital hole determined by the azide pi-plane in the latter complex, which is ca. 90° in-plane rotated from that of the imidazole pi-plane | Homo sapiens | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| heme oxygenase 1 | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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