Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur 
bond cleavage

Lago-Maciel, Ana; Soares, Jessica C; Zarzycki, Jan; Buchanan, Charles James; Reif-Trauttmansdorff, Tristan; Schmidt, Frederik V.; Lometto, Stefano; Paczia, Nicole; Schuller, Jan M; Hansen, D Flemming; Heller, Gabriella T; Prinz, Simone; Hochberg, Georg K. A.; Pierik, Antonio J; Rebelein, Johannes G.

doi:10.1101/2024.10.19.619033

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Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage

MPS-Authors

Lago-Maciel, Ana
Emmy Noether research Group Microbial Metalloenzymes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Zarzycki, Jan
Cellular Operating Systems, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Buchanan, Charles James
Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Schmidt, Frederik V.
Emmy Noether research Group Microbial Metalloenzymes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Lometto, Stefano
Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Paczia, Nicole
Core Facility Metabolomics and small Molecules Mass Spectrometry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Hochberg, Georg K. A.
Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Rebelein, Johannes G.
Emmy Noether research Group Microbial Metalloenzymes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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https://doi.org/10.1101/2024.10.19.619033
(Preprint)

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Citation

Lago-Maciel, A., Soares, J. C., Zarzycki, J., Buchanan, C. J., Reif-Trauttmansdorff, T., Schmidt, F. V., et al. (2024). Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage. bioRxiv: the preprint server for biology, 2024.10.19.619033. doi:10.1101/2024.10.19.619033.

Cite as: https://hdl.handle.net/21.11116/0000-000F-F4AA-E

Abstract

Methylthio-alkane reductases convert methylated sulfur compounds to methanethiol and small hydrocarbons, a process with important environmental and biotechnological implications. These enzymes are classified as nitrogenase-like enzymes, despite lacking the ability to convert dinitrogen to ammonia, raising fundamental questions about the factors controlling their activity and specificity. Here, we present the first molecular structure of the methylthio-alkane reductase, which reveals large metalloclusters, including the P-cluster and the [Fe8S9C]-cluster, previously only found in nitrogenases. Our findings suggest that distinct metallocluster coordination, surroundings, and substrate channels, determine the activity of these related metalloenzymes. This study provides new insights into nitrogen fixation, sulfur-compound reduction, and hydrocarbon production. We also shed light on the evolutionary history of P-cluster and [Fe8S9C]-cluster-containing reductases emerging prior to nitrogenases.Competing Interest StatementThe authors have declared no competing interest.