Soluble methane monooxygenase

Rahul Banerjee, Jason C. Jones, John D. Lipscomb

Research output: Contribution to journalArticlepeer-review

117 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)409-431
Number of pages23
JournalAnnual Review of Biochemistry
StatePublished - Jun 20 2019

Bibliographical note

Publisher Copyright:
© 2019 by Annual Reviews. All rights reserved.


  • crystallography
  • kinetics
  • methane
  • monooxygenase
  • oxygen activation
  • spectroscopy


Dive into the research topics of 'Soluble methane monooxygenase'. Together they form a unique fingerprint.

Cite this