nitrous-oxide reductase

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For detailed information about nitrous-oxide reductase, go to the full flat file.

Word Map on EC


+ 2 ferricytochrome c =
Nitrous oxide
+ 2 ferrocytochrome c + 2 H+


HdN2OR, McoP, MhN2OR, multicopper oxidase, N(2)OR, N2O reductase, N2OR, nitrous oxide reductase, NosZ, PpN2OR, PsN2OR, Sden_2219, SdN2OR, Z-type N2OR


     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.2 With a cytochrome as acceptor
       nitrous-oxide reductase


Crystallization on EC - nitrous-oxide reductase

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hanging drop vapour diffusion method
2.4 A resolution, preliminary study
1.6 A resolution
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
modeling of structure. The residues contributing to the semiocclusion of the T1 copper site are Trp355, Met389, and Met297. There is a negatively charged residue in the neighborhood of the T1 site, Glu296
purified enzyme, sitting drop vapor diffusion method, for His6-tagged Ca2+-bound apo-N2OR enzyme: mixing of 0.0003 ml of 15mg/ml protein solution with 0.0003 ml of well solution containing PEG 3350, 0.2 M ammonium sulfate, and 0.1 M Bis-Tris-HCl, pH 5.5, for Strep-tagged Ca2+-free or -bound apo-N2OR: mixing of 0.0003 ml of 15mg/ml protein solution with 0.0003 ml of well solution containing 25% w/v PEG 3350, 0.2 M lithium sulfate monohydrate, and 0.1 M Tris-HCl, pH 8.5, 7 days, 25°C, X-ray diffraction structure determination and analysis, molecular replacement and modelling using structure PDB ID 3SBQ as template. No crystals are obtained for Ca2+-free His6-tagged apo-N2OR