2025-10-31 マックス・プランク研究所
In the absence of oxygen, the enzyme methylthioalkane reductase produced by the bacterium Rhodospirillum rubrum generates ethylene, an essential component in the production of plastics, without releasing carbon dioxide.© MPI f. Terrestrial Microbiology/ Geisel
<関連情報>
- https://www.mpg.de/25460172/0925-terr-a-microbial-strategy-for-the-renewable-production-of-plastic-components-153410-x
- https://www.nature.com/articles/s41929-025-01426-2
メチルチオアルカン還元酵素は窒素固定酵素メタロクラスターを用いて炭素-硫黄結合を切断する Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage
Ana Lago-Maciel,Jéssica C. Soares,Jan Zarzycki,Charles J. Buchanan,Tristan Reif-Trauttmansdorff,Frederik V. Schmidt,Stefano Lometto,Nicole Paczia,Jan M. Schuller,D. Flemming Hansen,Gabriella T. Heller,Simone Prinz,Georg K. A. Hochberg,Antonio J. Pierik & Johannes G. Rebelein
Nature Catalysis Published:23 October 2025
DOI:https://doi.org/10.1038/s41929-025-01426-2
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 molecular structure of the methylthio-alkane reductase, which reveals large metalloclusters, including the P-cluster and the [Fe8S9C]-cluster, previously found only 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 before nitrogenases.
