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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 ligands modeled in the X-ray structure as OH(-) or H(2)O. However, elemental analyses and resonance Raman spectroscopy of isotopically labeled enzyme conclusively demonstrate that Cu(Z) has one acid-labile sulfur ligand. Thus, nitrous oxide reductase contains the first reported biological copper-sulfide cluster.

Type

Journal article

Journal

Biochemistry

Publication Date

24/10/2000

Volume

39

Pages

12753 - 12756

Keywords

Acids, Catalytic Domain, Circular Dichroism, Copper, Crystallization, Dimerization, Electron Spin Resonance Spectroscopy, Ligands, Magnetics, Oxidoreductases, Pseudomonas, Spectrum Analysis, Sulfides, Sulfur, X-Rays