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TitleMethylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.
Journal, issue, pagesNat Catal, Vol. 8, Issue 10, Page 1086-1099, Year 2025
Publish dateOct 23, 2025
AuthorsAna 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 /
PubMed AbstractMethylthio-alkane reductases convert methylated sulfur compounds to methanethiol and small hydrocarbons, a process with important environmental and biotechnological implications. These enzymes are ...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.
External linksNat Catal / PubMed:41140912 / PubMed Central
MethodsEM (single particle)
Resolution2.71 Å
Structure data

50553

9fmg

EMDB-50553, PDB-9fmg:
Methylthio-alkane reductase complex
Method: EM (single particle) / Resolution: 2.71 Å

Chemicals

ChemComp-S5Q:
FeFe cofactor

ChemComp-CLF:
FE(8)-S(7) CLUSTER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-AF3:
ALUMINUM FLUORIDE

ChemComp-SF4:
IRON/SULFUR CLUSTER

Source
  • rhodospirillum rubrum (bacteria)
KeywordsOXIDOREDUCTASE / Methylthioethanol / dimethyl sulfide / ethylmethyl sulfide / methanethiol / ethylene / methane / ethane / metalloenzyme

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