Heme-containing oxygenases
Article Abstract:
Heme-containing oxygenases catalyze the reaction of dioxygen with organic substrates by overcoming the high kinetic energy barrier associated with the dioxygen triplet ground state. The structure of these enzymes varies from ferryl-oxo porphyrin pi-cation radical to ferric-peroxide. Cysteine releases the electron required for dioxygen activation to produce oxo-iron reactive oxygen intermediates. Indoleamine and tryptophan dioxygenases are ferrous-dioxygen adducts that directly incorporate two dioxygen atoms by an ionic mechanism to form oxygenated products.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
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Reaction mechanisms of mononuclear non-heme iron oxygenases
Article Abstract:
An analysis of results obtained since the year 1999 from primary sequences, structure-function relationships, and chemical kinetics and mechanisms dealing with mononuclear non-heme iron inter- an intramolecular dioxygenases is presented. The versatility of non-heme iron centers in biological oxidations is evident from the reactions they catalyze.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2005
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Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates
Article Abstract:
The advances in the understanding of molecular nonheme iron oxygenases are discussed. The binding of dioxygen leads to an adduct with significant iron (III) superoxide radical anion character.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2004
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