N2O binding at a [4Cu:2S] copper–sulphur cluster in nitrous oxide reductase

Anja Pomowski, Walter G. Zumft, Peter M. H. Kroneck and Oliver Einsle ()
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Anja Pomowski: Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21
Walter G. Zumft: Institut für Angewandte Biowissenschaften, Karlsruher Institut für Technologie, Hertzstr. 16
Peter M. H. Kroneck: Fachbereich Biologie, Universität Konstanz, Universitätsstr. 10
Oliver Einsle: Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21

Nature, 2011, vol. 477, issue 7363, 234-237

Abstract: N2O reductase form and function Nitrous oxide (N2O) gas, generated by both natural and anthropogenic processes, is a potentially important greenhouse gas because of its heat-trapping effects and its persistence in the atmosphere. Some bacteria use nitrous oxide reductase (N2OR) to convert N2O to dinitrogen gas. The X-ray crystal structure of N2OR from Pseudomonas stutzeri has now been determined in the presence of N2O and, to generate the active purple form of the enzyme, in the absence of O2. The results reveal the nature of the copper–sulphur cluster at the substrate-binding site and show how N2O interacts with this complex metal centre.

Date: 2011
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DOI: 10.1038/nature10332

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