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Literature summary for 1.14.99.58 extracted from
- The hydrogen-bonding network in heme oxygenase also functions as a modulator of enzyme dynamics: chaotic motions upon disrupting the H-bond network in heme oxygenase from Pseudomonas aeruginosa (2007), J. Am. Chem. Soc., 129, 11730-11742.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| Carr-Purcell-Meiboom-Gill NMR study on ferric enzyme state inhibited by cyanide and azide, and its ferrous state inhibited by carbon monoxide. The nature of the coordinated distal ligand affects the conformational freedom of the polypeptide in regions of the enzyme far removed from the heme iron and distal ligand. In addition to proton delivery to the nascent FeIII-OO- intermediate during catalysis, the hydrogen-bonding network serves to propagate the electronic state in each of the distinct steps of the catalytic cycle to key but remote sections of the polypeptide and to modulate the conformational freedom of the enzyme | Pseudomonas aeruginosa |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R80L | mutant exhibits allmost global conformational disorder related to significantly lower efficiency to hydroxylate heme in the presence of H2O2 | Pseudomonas aeruginosa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
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Release 2023.1 (January 2023)
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