Cloned (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
W66A | steric bulk at residue 66 promotes MhuD-catalyzed heme oxygenation, and this reaction does not depend upon the generation of free peroxide. The protein fold is similar to wild-type | Mycobacterium tuberculosis |
W66F | steric bulk at residue 66 promotes MhuD-catalyzed heme oxygenation, and this reaction does not depend upon the generation of free peroxide. The protein fold is similar to wild-type | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WKH3 | - |
- |
Mycobacterium tuberculosis ATCC 25618 | P9WKH3 | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | small amounts of heme ruffling have no influence on the energy of the Q-band and blue-shift the Soret band due to symmetry-allowed mixing of the Fe 3dxy and porphyrin a2u orbitals. Larger amounts of ruffling red-shift both the Q and Soret bands due to disruption of pi-bonding within the porphyrin ring | Mycobacterium tuberculosis |