Molecular interplay of an assembly machinery for nitrous oxide reductase

Christoph Müller, Lin Zhang, Sara Zipfel, Annika Topitsch, Marleen Lutz, Johannes Eckert, Benedikt Prasser, Mohamed Chami, Wei Lü, Juan Du () and Oliver Einsle ()
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Christoph Müller: Albert-Ludwigs-Universität Freiburg
Lin Zhang: Albert-Ludwigs-Universität Freiburg
Sara Zipfel: Albert-Ludwigs-Universität Freiburg
Annika Topitsch: Albert-Ludwigs-Universität Freiburg
Marleen Lutz: Albert-Ludwigs-Universität Freiburg
Johannes Eckert: Albert-Ludwigs-Universität Freiburg
Benedikt Prasser: Albert-Ludwigs-Universität Freiburg
Mohamed Chami: Universität Basel
Wei Lü: Van Andel Institute
Juan Du: Van Andel Institute
Oliver Einsle: Albert-Ludwigs-Universität Freiburg

Nature, 2022, vol. 608, issue 7923, 626-631

Abstract: Abstract Emissions of the critical ozone-depleting and greenhouse gas nitrous oxide (N2O) from soils and industrial processes have increased considerably over the last decades1–3. As the final step of bacterial denitrification, N2O is reduced to chemically inert N2 (refs. 1,4) in a reaction that is catalysed by the copper-dependent nitrous oxide reductase (N2OR) (ref. 5). The assembly of its unique [4Cu:2S] active site cluster CuZ requires both the ATP-binding-cassette (ABC) complex NosDFY and the membrane-anchored copper chaperone NosL (refs. 4,6). Here we report cryo-electron microscopy structures of Pseudomonas stutzeri NosDFY and its complexes with NosL and N2OR, respectively. We find that the periplasmic NosD protein contains a binding site for a Cu+ ion and interacts specifically with NosL in its nucleotide-free state, whereas its binding to N2OR requires a conformational change that is triggered by ATP binding. Mutually exclusive structures of NosDFY in complex with NosL and with N2OR reveal a sequential metal-trafficking and assembly pathway for a highly complex copper site. Within this pathway, NosDFY acts as a mechanical energy transducer rather than as a transporter. It links ATP hydrolysis in the cytoplasm to a conformational transition of the NosD subunit in the periplasm, which is required for NosDFY to switch its interaction partner so that copper ions are handed over from the chaperone NosL to the enzyme N2OR.

Date: 2022
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DOI: 10.1038/s41586-022-05015-2

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