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A [3Cu:2S] cluster provides insight into the assembly and function of the Cu<sub>Z</sub> site of nitrous oxide reductase

A [3Cu:2S] cluster provides insight into the assembly and function of the CuZ site of nitrous oxide reductase

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ZHANG, Lin, Eckhard BILL, Peter M. H. KRONECK, Oliver EINSLE, 2021. A [3Cu:2S] cluster provides insight into the assembly and function of the CuZ site of nitrous oxide reductase. In: Chemical Science. Royal Society of Chemistry (RSC). 12(9), pp. 3239-3244. ISSN 2041-6520. eISSN 2041-6539. Available under: doi: 10.1039/d0sc05204c

@article{Zhang2021-03-113Cu2S-53611, title={A [3Cu:2S] cluster provides insight into the assembly and function of the CuZ site of nitrous oxide reductase}, year={2021}, doi={10.1039/d0sc05204c}, 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} }

A [3Cu:2S] cluster provides insight into the assembly and function of the Cu<sub>Z</sub> site of nitrous oxide reductase Einsle, Oliver 2021-03-11 Kroneck, Peter M. H. 2021-05-06T11:42:58Z Bill, Eckhard Zhang, Lin eng Einsle, Oliver Bill, Eckhard Zhang, Lin Attribution-NonCommercial 3.0 Unported 2021-05-06T11:42:58Z Kroneck, Peter M. H. Nitrous oxide reductase (N<sub>2</sub>OR) is the only known enzyme reducing environmentally critical nitrous oxide (N<sub>2</sub>O) to dinitrogen (N<sub>2</sub>) as the final step of bacterial denitrification. The assembly process of its unique catalytic [4Cu:2S] cluster Cu<sub>Z</sub> 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<sub>2</sub>OR in Escherichia coli. While no copper ion was found in the Cu<sub>Z</sub> 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<sub>Z2</sub>, 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<sub>Z2</sub> may have been observed before, but not recognized. The sulfide shift changes the metal coordination in Cu<sub>Z</sub> and is thus of high mechanistic interest.

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