Crystal structure of a key enzyme for anaerobic ethane activation

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Abstract
How to feed an enzyme ethane: When released from ocean floor seeps, small hydrocarbons are rapidly consumed by micro-organisms. Methane is highly abundant and is both produced and consumed by microbes through well understood biochemical pathways. Less well understood is how ethane, also a major natural component of gaseous hydrocarbons, is metabolized. To understand how microbes take advantage of this energy and carbon source, Hahn et al. solved the x-ray crystal structures of an enzyme they call ethyl coenzyme-M reductase, which converts ethane into the thioether ethyl-coenzyme M as the entry point for catabolism. They found an expanded active site and, using a xenon gas derivatization experiment, a distinctive tunnel through the protein that is proposed to permit access of the gaseous substrate. Science , abg1765, this issue p. 118
Funding Information
  • National Science Foundation (1357238)
  • Deutsche Forschungsgemeinschaft (EXC-2077 – 390741603)
  • Swiss National Science Foundation (200021_182369)
  • Max Planck Gesellschaft

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