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Literature summary for 1.7.2.4 extracted from

  • Ertem, M.Z.; Cramer, C.J.; Himo, F.; Siegbahn, P.E.
    N-O bond cleavage mechanism(s) in nitrous oxide reductase (2012), J. Biol. Inorg. Chem., 17, 687-698.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
building of two models of the active site reveals two distinct mechanisms. In the first model, N2O binds to the fully reduced tetranuclear Cu4S core in a bent my-(1,3)-O,N bridging fashion between the CuI and CuIV centres and subsequently extrudes N2 while generating the corresponding bridged my-oxo species. In the second model, substrate N2O binds loosely to one of the coppers of the tetranuclear Cu4S core in a terminal fashion, i.e., using only the oxygen atom. Loss of N2 generates the same my-oxo copper core. The free energies of activation predicted for these two alternative pathways are close to one another and do not provide decisive support for one over the other Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans Q51705
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Synonyms

Synonyms Comment Organism
NosZ
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Paracoccus denitrificans