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Literature summary for 1.1.9.1 extracted from

  • De Jong, G.A.H.; Caldeira, J.; Sun, J.; Jongejan, J.A.; de Vries, S.; Loehr, T.M.; Moura, I.; Moura, J.J.G.; Duine, J.A.
    Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni (1995), Biochemistry, 34, 9451-9458.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
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Cofactor

Cofactor Comment Organism Structure
heme binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer Comamonas testosteroni
pyrroloquinoline quinone binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer Comamonas testosteroni