The catalytic center in nitrous oxide reductase, Cu-z, is a copper-sulfide cluster

Tim Rasmussen, B C Berks, J Sanders-Loehr, D M Dooley, W G Zumft, A J Thomson

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115 Citations (Scopus)

Abstract

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 H2O. 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.

Original languageEnglish
Pages (from-to)12753-12756
Number of pages4
JournalBiochemistry
Volume39
Issue number42
DOIs
Publication statusPublished - 24 Oct 2000

Keywords

  • ELECTRON-TRANSFER CENTER
  • PSEUDOMONAS-PERFECTOMARINA
  • PARACOCCUS-DENITRIFICANS
  • MULTICOPPER ENZYME
  • A CENTER
  • PURIFICATION
  • SPECTROSCOPY
  • PROTEINS
  • STUTZERI
  • SULFUR
  • ELECTRON TRANSFER CENTER

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