1.7.2.4: nitrous-oxide reductase

This is an abbreviated version!
For detailed information about nitrous-oxide reductase, go to the full flat file.

Word Map on EC 1.7.2.4

Reaction

nitrogen
+
H2O
+ 2 ferricytochrome c =
Nitrous oxide
+ 2 ferrocytochrome c + 2 H+

Synonyms

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

ECTree

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

Crystallization

Crystallization on EC 1.7.2.4 - nitrous-oxide reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
-
2.4 A resolution, preliminary study
-
1.6 A resolution
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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
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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
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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