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BRENDA support

Literature summary for 1.7.2.5 extracted from

  • Kapetanaki, S.M.; Field, S.J.; Hughes, R.J.; Watmough, N.J.; Liebl, U.; Vos, M.H.
    Ultrafast ligand binding dynamics in the active site of native bacterial nitric oxide reductase (2008), Biochim. Biophys. Acta, 1777, 919-924.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains heme and non-heme iron Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans
-
-
-

Synonyms

Synonyms Comment Organism
nitric oxide reductase
-
Paracoccus denitrificans
NOR
-
Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
heme heme-ligand recombination in this enzyme is considerably faster than in heme-copper oxidases and is consistent with a more confined configuration of the active site Paracoccus denitrificans