| Literature DB >> 11041839 |
T Rasmussen1, B C Berks, J Sanders-Loehr, D M Dooley, W G Zumft, A J Thomson.
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 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.Entities:
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Year: 2000 PMID: 11041839 DOI: 10.1021/bi001811i
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162