Soluble Methane Monooxygenase

Annu Rev Biochem. 2019 Jun 20;88:409-431. doi: 10.1146/annurev-biochem-013118-111529. Epub 2019 Jan 11.


Aerobic life is possible because the molecular structure of oxygen (O2) makes direct reaction with most organic materials at ambient temperatures an exceptionally slow process. Of course, these reactions are inherently very favorable, and they occur rapidly with the release of a great deal of energy at high temperature. Nature has been able to tap this sequestered reservoir of energy with great spatial and temporal selectivity at ambient temperatures through the evolution of oxidase and oxygenase enzymes. One mechanism used by these enzymes for O2 activation has been studied in detail for the soluble form of the enzyme methane monooxygenase. These studies have revealed the step-by-step process of O2 activation and insertion into the ultimately stable C-H bond of methane. Additionally, an elegant regulatory mechanism has been defined that enlists size selection and quantum tunneling to allow methane oxidation to occur specifically in the presence of more easily oxidized substrates.

Keywords: crystallography; kinetics; methane; monooxygenase; oxygen activation; spectroscopy.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Bacteria / enzymology*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Crystallography
  • Kinetics
  • Methane / metabolism*
  • Methylococcus capsulatus / enzymology
  • Methylosinus trichosporium / enzymology
  • Oxygen / metabolism*
  • Oxygenases / chemistry
  • Oxygenases / metabolism*
  • Protein Conformation


  • Bacterial Proteins
  • Oxygenases
  • methane monooxygenase
  • Methane
  • Oxygen