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Title: A nitrogenase-like enzyme system catalyzes methionine, ethylene, and methane biogenesis

Journal Article · · Science (Online)
ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [3]; ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [4]; ORCiD logo [2]; ORCiD logo [3]; ORCiD logo [1]
  1. The Ohio State Univ., Columbus, OH (United States)
  2. Colorado State Univ., Fort Collins, CO (United States)
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Chemical Sciences Division
  4. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)

Bacterial production of gaseous hydrocarbons such as ethylene and methane affects soil environments and atmospheric climate. We demonstrate that biogenic methane and ethylene from terrestrial and freshwater bacteria are directly produced by a previously unknown methionine biosynthesis pathway. This pathway, present in numerous species, uses a nitrogenase-like reductase that is distinct from known nitrogenases and nitrogenase-like reductases and specifically functions in C–S bond breakage to reduce ubiquitous and appreciable volatile organic sulfur compounds such as dimethyl sulfide and (2-methylthio)ethanol. Liberated methanethiol serves as the immediate precursor to methionine, while ethylene or methane is released into the environment. Anaerobic ethylene production by this pathway apparently explains the long-standing observation of ethylene accumulation in oxygen-depleted soils. Methane production reveals an additional bacterial pathway distinct from archaeal methanogenesis.

Research Organization:
The Ohio State Univ., Columbus, OH (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER); NCI
Contributing Organization:
University of Colorado Cancer Center’s Genomics and Microarray Core Shared Resource; University of Colorado Boulder Research Computing Group; Environmental Molecular Sciences Laboratory; Battelle and UT-Battelle, LLC
Grant/Contract Number:
SC0019338; AC05-76RLO1830; P30CA046934; AC05-00OR22725
OSTI ID:
1658249
Alternate ID(s):
OSTI ID: 1813253
Journal Information:
Science (Online), Vol. 369, Issue 6507; Related Information: All raw mass spectraand searched data files for the proteome measurements have beendeposited into the ProteomeXchange repository: MassIVE accessionnumber MSV000084455 (FTP link to files: ftp://massive.ucsd.edu/MSV000084455/) and ProteomeXchange accession numberPXD015818. Raw transcriptomics reads are available in the NCBISequence Read Archive under accession numbers SRR10887327through SRR10887338 and BioProject accession number PRJNA601207.; ISSN 1095-9203
Publisher:
AAASCopyright Statement
Country of Publication:
United States
Language:
English

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