The Catalytic Center in Nitrous Oxide Reductase, CuZ, Is a Copper−Sulfide Cluster
| Autor: | Ben C. Berks, Tim Rasmussen, Joann Sanders-Loehr, Walter G. Zumft, Andrew J. Thomson, David M. Dooley |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
inorganic chemicals
Denitrification Resonance Raman spectroscopy Inorganic chemistry chemistry.chemical_element Nitrous-oxide reductase Sulfides Ligands Biochemistry Catalysis Magnetics chemistry.chemical_compound Catalytic Domain Pseudomonas Polymer chemistry biology Circular Dichroism Spectrum Analysis X-Rays Electron Spin Resonance Spectroscopy Nitrous oxide biology.organism_classification Copper Sulfur chemistry Paracoccus denitrificans Crystallization Oxidoreductases Acids Dimerization |
| Zdroj: | Biochemistry. 39:12753-12756 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi001811i |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|