Detection and localization of two hydrogenases in Methylococcus capsulatus (Bath) and their potential role in methane metabolism

Arch Microbiol. 2002 Feb;177(2):167-72. doi: 10.1007/s00203-001-0372-4. Epub 2001 Nov 30.

Abstract

Methylococcus capsulatus (Bath) was shown to contain two distinct hydrogenases, a soluble hydrogenase and a membrane-bound hydrogenase. This is the first report of a membrane-bound hydrogenase in methanotrophs. Both enzymes were expressed apparently constitutively under normal growth conditions. The soluble hydrogenase was capable of reducing NAD(+) with molecular hydrogen. The activities of both soluble and particulate methane monooxygenases could be driven by molecular hydrogen. This confirmed that molecular hydrogen could be used as a source of reducing power for methane oxidation. Hydrogen-driven methane monooxygenase activities tolerated elevated temperatures and moderate oxygen concentrations. The significance of these findings for biotechnological applications of methanotrophs is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrogen / metabolism
  • Hydrogenase / isolation & purification*
  • Methane / metabolism
  • Methylococcus capsulatus / enzymology*
  • Oxidoreductases / isolation & purification
  • Oxygenases / metabolism

Substances

  • Hydrogen
  • Oxidoreductases
  • nickel-iron hydrogenase
  • hydrogen dehydrogenase
  • Hydrogenase
  • Oxygenases
  • methane monooxygenase
  • Methane