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Literature summary for 7.1.1.7 extracted from

  • Paulus, A.; Rossius, S.G.; Dijk, M.; de Vries, S.
    Oxoferryl-porphyrin radical catalytic intermediate in cytochrome bd oxidases protects cells from formation of reactive oxygen species (2012), J. Biol. Chem., 287, 8830-8838.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABJ9 subunit cydA
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information after the initial binding of O2, the O–O bond is heterolytically cleaved to yield a kinetically competent heme d oxoferryl porphyrin pi-cation radical intermediate magnetically interacting with heme b595. This intermediate accumulates to 0.75-0.85 per enzyme in agreement with its much higher rate of formation at 20000 per s compared with its rate of decay of 1900 per s. The intermediate is next converted to a short lived heme d oxoferryl in a phase kinetically matched to the oxidation of heme b558 before completion of the reaction. The results indicate that cytochrome bd oxidases break the O-O bond in a single four-electron transfer without a peroxide intermediate. The fourth electron is donated by the porphyrin moiety rather than by a nearby amino acid Escherichia coli ?
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