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Literature summary for 1.14.99.57 extracted from

  • Graves, A.B.; Graves, M.T.; Liptak, M.D.
    Measurement of heme ruffling changes in MhuD using UV-vis pectroscopy (2016), J. Phys. Chem. B, 120, 3844-3853.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Mycobacterium tuberculosis

Protein Variants

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WKH3
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Mycobacterium tuberculosis ATCC 25618 P9WKH3
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Cofactor

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