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Nitrous oxide reductase catalyses the reduction of nitrous oxide to dinitrogen at a unique tetranuclear copper site, called Cu(Z), which has a central inorganic sulphide ligand. Limited incubation with oxygen during the preparation of nitrous oxide reductase from Paracoccus pantotrophus results in changed redox properties of the catalytic centre by comparison with anaerobic preparations. While the anaerobically purified enzyme has a catalytic centre which performs a single electron step at a midpoint potential of E(m)=+60 mV versus the standard hydrogen electrode (n=1), the altered centre shows no redox change under similar experimental conditions. Spectroscopic properties of this 'redox fixed' centre are similar to spectra of the reduced 'redox active' form of CuZ, although the positions and intensities of a number of transitions are changed in the optical spectrum. These observations are interpreted in terms of two forms of the catalytic centre, called CuZ and CuZ*. The structural relationship between these forms is unclear. EPR and magnetic circular dichroism spectra suggest that the basic Cu4S structure is common to both. Curiously, steady-state activity of the aerobic enzyme preparation is slightly increased despite the fact the catalytic centre does not undergo detectable redox changes.

Original publication




Journal article


Biochem J

Publication Date





807 - 815


Catalytic Domain, Circular Dichroism, Copper, Isoenzymes, Kinetics, Oxidation-Reduction, Oxidoreductases, Paracoccus, Protein Conformation, Spectrophotometry, Zinc