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Literature summary for 1.11.1.10 extracted from

  • Dawson, J.H.; Kau, L.S.; Penner-Hahn, J.E.; Sono, M.; Smith Eble, K.; Bruce, G.S.; Hager, L.P.; Hodgson, K.O.
    Oxygenated cytochrome P-450-CAM and chloroperoxidase: direct evidence for sulfur donor ligation trans to dioxygen and structural characterization using EXAFS spectroscopy (1986), J. Am. Chem. Soc., 108, 8114-8116.
No PubMed abstract available

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A Leptoxyphium fumago ?
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Cofactor

Cofactor Comment Organism Structure
heme the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A Leptoxyphium fumago