@article{Zhang2021-03-113Cu2S-53611,
  year={2021},
  doi={10.1039/d0sc05204c},
  title={A [3Cu:2S] cluster provides insight into the assembly and function of the Cu<sub>Z</sub> site of nitrous oxide reductase},
  number={9},
  volume={12},
  issn={2041-6520},
  journal={Chemical Science},
  pages={3239--3244},
  author={Zhang, Lin and Bill, Eckhard and Kroneck, Peter M. H. and Einsle, Oliver}
}

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    <dc:creator>Einsle, Oliver</dc:creator>
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    <dcterms:abstract xml:lang="eng">Nitrous oxide reductase (N&lt;sub&gt;2&lt;/sub&gt;OR) is the only known enzyme reducing environmentally critical nitrous oxide (N&lt;sub&gt;2&lt;/sub&gt;O) to dinitrogen (N&lt;sub&gt;2&lt;/sub&gt;) as the final step of bacterial denitrification. The assembly process of its unique catalytic [4Cu:2S] cluster Cu&lt;sub&gt;Z&lt;/sub&gt; remains scarcely understood. Here we report on a mutagenesis study of all seven histidine ligands coordinating this copper center, followed by spectroscopic and structural characterization and based on an established, functional expression system for Pseudomonas stutzeri N&lt;sub&gt;2&lt;/sub&gt;OR in Escherichia coli. While no copper ion was found in the Cu&lt;sub&gt;Z&lt;/sub&gt; binding site of variants H129A, H130A, H178A, H326A, H433A and H494A, the H382A variant carried a catalytically inactive [3Cu:2S] center, in which one sulfur ligand, S&lt;sub&gt;Z2&lt;/sub&gt;, had relocated to form a weak hydrogen bond to the sidechain of the nearby lysine residue K454. This link provides sufficient stability to avoid the loss of the sulfide anion. The UV-vis spectra of this cluster are strikingly similar to those of the active enzyme, implying that the flexibility of S&lt;sub&gt;Z2&lt;/sub&gt; may have been observed before, but not recognized. The sulfide shift changes the metal coordination in Cu&lt;sub&gt;Z&lt;/sub&gt; and is thus of high mechanistic interest.</dcterms:abstract>
    <dc:creator>Bill, Eckhard</dc:creator>
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    <dcterms:title>A [3Cu:2S] cluster provides insight into the assembly and function of the Cu&lt;sub&gt;Z&lt;/sub&gt; site of nitrous oxide reductase</dcterms:title>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-05-06T11:42:58Z</dc:date>
    <dc:contributor>Bill, Eckhard</dc:contributor>
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    <dc:rights>Attribution-NonCommercial 3.0 Unported</dc:rights>
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    <dc:creator>Zhang, Lin</dc:creator>
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    <dc:contributor>Einsle, Oliver</dc:contributor>
    <dc:contributor>Zhang, Lin</dc:contributor>
    <dc:contributor>Kroneck, Peter M. H.</dc:contributor>
    <dcterms:issued>2021-03-11</dcterms:issued>
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    <dc:creator>Kroneck, Peter M. H.</dc:creator>
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