9FMG

Methylthio-alkane reductase complex

9FMG の概要

• エントリーDOI: 10.2210/pdb9fmg/pdb
• EMDBエントリー: 50553
• 分子名称: Nitrogenase, Nitrogenase iron protein, FeFe cofactor, ... (9 entities in total)
• 機能のキーワード: methylthioethanol, dimethyl sulfide, ethylmethyl sulfide, methanethiol, ethylene, methane, ethane, metalloenzyme, oxidoreductase
• 由来する生物種: Rhodospirillum rubrum; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 225943.49

構造登録者

Lago-Maciel, A.,Zarzycki, J.,Prinz, S.,Reif-Trauttmansdorff, T.,Rebelein, J.G. (登録日: 2024-06-06, 公開日: 2025-09-17, 最終更新日: 2026-04-01)

主引用文献

Lago-Maciel, A.,Soares, J.C.,Zarzycki, J.,Buchanan, C.J.,Reif-Trauttmansdorff, T.,Schmidt, F.V.,Lometto, S.,Paczia, N.,Schuller, J.M.,Hansen, D.F.,Heller, G.T.,Prinz, S.,Hochberg, G.K.A.,Pierik, A.J.,Rebelein, J.G.
Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.
Nat Catal, 8:1086-1099, 2025

PubMed 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 [FeSC]-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 [FeSC]-cluster-containing reductases emerging before nitrogenases.

PubMed: 41140912
DOI: 10.1038/s41929-025-01426-2

実験手法

ELECTRON MICROSCOPY (2.71 Å)