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.

Observations, Oxidation-reduction reaction, Oxidation-reduction reactions, Heme

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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.

Analysis, Biodegradation, Chemical reaction, Rate of, Chemical kinetics

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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.

Iron compounds, Chemical properties

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