The catalytic center in nitrous oxide reductase, CuZ, is a copper-sulfide cluster.
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.
Rasmussen
T
T
Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, and School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
Berks
B C
BC
Sanders-Loehr
J
J
Dooley
D M
DM
Zumft
W G
WG
Thomson
A J
AJ
D000143:Acids; D020134:Catalytic Domain; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry*; D003460:Crystallization; D019281:Dimerization; D004578:Electron Spin Resonance Spectroscopy; D008024:Ligands; D008280:Magnetics; D010088:Oxidoreductases / Q000737:chemistry*; D011549:Pseudomonas / Q000201:enzymology; D013057:Spectrum Analysis; D013440:Sulfides / Q000737:chemistry*; D013455:Sulfur / Q000737:chemistry; D014965:X-Rays
D000143:Acids; D008024:Ligands; D013440:Sulfides; D013455:Sulfur; D003300:Copper; D010088:Oxidoreductases; C022763:nitrous oxide reductase