The crystal structure of nitrous oxide reductase, the enzyme catalyzing the
final step of bacterial denitrification in which nitrous oxide is reduced
to dinitrogen, exhibits a novel catalytic site, called Cu-z. This comprises
a cluster of four copper ions bound by seven histidines and three other li
gands modeled in the X-ray structure as OH- or H2O. However, elemental anal
yses and resonance Raman spectroscopy of isotopically labeled enzyme conclu
sively demonstrate that Cu-z has one acid-labile sulfur ligand. Thus, nitro
us oxide reductase contains the first reported biological copper-sulfide cl
uster.