Sulphur Atoms in the Metal Centre
A team of researchers has discovered a new binding site for nitrous oxide (N2O)
The functionality and mechanisms of this important enzyme had not been thoroughly researched until Dr Anja Pomowski successfully clarified the structure of a N2O reductase, primed under the strict exclusion of dioxygen (02). Dr Pomowski belongs to the research group headed by Prof Dr Oliver Einsle, a professor at the Institute of Organic Chemistry and Biochemistry of the University of Freiburg and a member of the BIOSS Cluster of Excellence. Together with Prof Dr Walter Zumft from the Karlsruhe Institute of Technology and Prof Dr Peter Kroneck from the University of Konstanz, the team of researchers is presenting their results in the current issue of the specialist journal Nature. The newly discovered structure shows first that the ratio and amount of substances in the metal centre of the enzyme have only been described incompletely thus far, and that they contain an additional sulphur atom. Second, the team also identified the binding of the N2O substrate to the metal centre. This binding site was a surprise to the scientists, and it has encouraged them to re-evaluate the mechanisms of the enzyme, whose molecular properties Prof Dr Oliver Einsle’s group will continue to research in the future.
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