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 language | English |
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Pages (from-to) | 12753-12756 |
Number of pages | 4 |
Journal | Biochemistry |
Volume | 39 |
Issue number | 42 |
DOIs | |
Publication status | Published - 24 Oct 2000 |
Keywords
- ELECTRON-TRANSFER CENTER
- PSEUDOMONAS-PERFECTOMARINA
- PARACOCCUS-DENITRIFICANS
- MULTICOPPER ENZYME
- A CENTER
- PURIFICATION
- SPECTROSCOPY
- PROTEINS
- STUTZERI
- SULFUR
- ELECTRON TRANSFER CENTER