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  • Methane monooxygenase, or MMO, is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes. Methane monooxygenase belongs to the class of oxidoreductase enzymes.
  • Methane monooxygenase comes in two varieties: soluble and membrane bound. The soluble MMO is very nonspecific and is present primarily in Type II methanotrophs, where it is induced by low copper conditions enzyme. The membrane bound or particulate MMO (pMMO) is constitutive, but limited by the availability of copper. It is more specific for methane and oxidizes fewer xenobiotics.
  • Methanotrophic bacteria are a unique family of gram negative eubacteria that utilize
    methane as their sole source of carbon and energy. The first step in their metabolic pathway is
    the oxidation of methane to methanol by methane monooxygenase (MMO) enzyme systems.
  • The particulate methane monooxygenase and related ammonia monooxygenase are integral membrane proteins, occurring in methanotrophs and ammonia oxidisers, respectively.
  • Particulate methane monooxygenase from Methylococcus capsulatus is an ABC homotrimer, which contains mononuclear and dinuclear copper metal centers, and a third metal center containing a metal ion whose identity in vivo is not certain.
  • Methane monooxygenases are found in methanotrophic bacteria, a class of bacteria that exist at the interface of aerobic and anaerobic environments.
  • Methane monooxygenase of methane-assimilating bacteria acts on C2-C4 to produce the corresponding epoxide using NADH as a cofactor. A bioreactor containing methane-assimilating bacteria was constructed for the production of propene oxide.
  • MMOs are found in methanotrophs, which are bacteria that appear to be ubiquitous in the environment and can grow with methane as the sole source of  carbon and energy.
  • The soluble methane monooxygenase from the pseudothermophile Methylococcus capsulatus
    (Bath) is a three-component enzyme system that catalyzes
    the selective oxidation of methane to methanol.
  • In order to obtain particulate methane monooxygenase (pMMO)-enriched membranes from Methylococcus
    capsulatus (Bath) with high activity and in high yields, a method is  devised  to process cell growth in a fermentor adapted with a hollow-fiber bioreactor that allows easy control and quantitative adjustment of the
    copper ion concentration in NMS medium over the time course of cell culture.
  • The soluble methane monooxygenase
    from Methylococcus capsulatus (Bath) is a three-component
    enzyme; the 251-kDa hydroxylase component (MMOH) contains
    a carboxylate-bridged dinuclear iron active site in each α subunit
    of an (αβγ)2 structure.
  • Soluble methane monooxygenase (sMMO) contains a
    nonheme, carboxylate-bridged diiron site that activates
    dioxygen in the catalytic oxidation of hydrocarbon substrates.
  • The use of enzymes known as methane monooxygenases to catalyse the oxidation of methane to methanol is a defining characteristic of methanotrophs.
  • This enzyme also
    has potential applications for converting waste methane
    into methanol, synthesizing homochiral epoxides, and
    probing the biochemical fundamentals of the methane
    oxidation reaction.
General Information
  • Methane Monooxygenase Data
  • Methylococcus Capsulatus
  • Methane Monooxygenase
  • Methane monooxygenase - Info


  • Crystal structure of particulate methane monooxygenase
  • Properties of a Soluble Methane Monooxygenase from a Facultative Methane- Utilizing Organism, Methylobacterium sp. Strain
  • Purification and Properties of the Hydroxylase Component of
    Methane Monooxygenase
  • Structure of the soluble methane monooxygenase regulatory
    protein B
  • Crystal structure of particulate methane monooxygenase

Analysis and Functions

  • Analysis of Methane Monooxygenase Genes
  • Characterization of MMOD, a long overlloked component of the soluble methane monooxygenase from methylococcus capsulatus
  • Homologous expression of soluble methane monooxygenase genes in Methylosinus trichosporium OB3b
  • Mutagenesis of the “Leucine Gate” To Explore the Basis of Catalytic Versatility in Soluble Methane Monooxygenase
  • Oxygen Kinetic Isotope Effects in Soluble Methane Monooxygenase
  • Role of multiple gene copies in particulate methane monooxygenase activity in the
    methane-oxidizing bacterium Methylococcus capsulatus Bath
  • Molecular sequencing and analysis of soluble methane monooxygenase gene clusters from methanotroph Methylomonas sp.
  • Structural Features of Covalently Cross-linked Hydroxylase and Reductase Proteins of Soluble Methane Monooxygenase as Revealed by Mass Spectrometric Analysis


  • Constitutive soluble methane monooxygenase mutants of methanotrophic bacteria such as Methylosinus trichosporium
  • Rapid degradation of halogenated hydrocarbons by soluble methane monooxygenase
  • Insertion sequence
  • Method for Oxidizing hydrocarbons with a hydroxylase from a Methane monooxygenase
  • Rapid Degradation of Halogenated Hydrocarbons by Soluble Methane Monooxygenase


  • Mechanisms of Metalloenzymes and Metallocofactor Assembly
  • Biodiversity of methanotrophs and their bioremediation and biotechnological exploitation (BOMBBE)
  • Domain Engineering of the Reductase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath)
  • Stabilizing a monooxygenase for use in environmental cleanup
  • Postgenomic studies on the methane oxidising bacterium Methylococcus capsulatus (Bath)


  • Converting Methane to Methanol: Structural Insight into the Reaction Center of Particulate Methane Monooxygenase
  • Optimization of Trichloroethylene
    Degradation Using Soluble Methane Monooxygenase
  • Microbial Production of Commodity Chemicals
  • Investigation of the copper-regulated expression of methane monooxygenases in  Methylococcus capsulatus (Bath)
  • The Copper Clusters in the Particulate Methane Monooxygenase (pMMO)
    from Methylococcus capsulatus (Bath)
  • Geometrical Variability in the Diferrous Active Site of the Soluble Methane Monooxygenase Hydroxylase from
    Methylococcus capsulatus (Bath)
  • Transient Intermediates of the Methane Monooxygenase Catalytic Cycle
  • Membrane-Associated Methane  Monooxygenase from Methylococcus capsulatus (Bath)
  • The Membrane-associated Form of Methane Monooxygenase from
    Methylococcus capsulatus (Bath) is a Copper/Iron Protein
  • Oxidation of Ultrafast Radical Clock Substrate Probes by the Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath)
  • The Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath) Is a Novel Copper-containing Three-subunit
  • Soluble Methane Monooxygenase Production and Trichloroethylene
    Degradation by a Type I Methanotroph,
    Methylomonas methanica
  • Production of High-Quality Particulate Methane Monooxygenase in
    High Yields from Methylococcus capsulatus (Bath) with a Hollow-Fiber Membrane Bioreactor
  • Protein B of Soluble Methane Monooxygenase from Methylococcus
    capsulatus (Bath)
  • Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster
  • Purification and Characterization of the Soluble Methane Monooxygenase of the Type II Methanotrophic Bacterium Methylocystis sp. Strain
  • Radiolytic Reduction of Methane Monooxygenase Dinuclear Iron Cluster at 77K
  • Soluble Methane Monooxygenase Gene Clusters from Trichloroethylene-Degrading Methylomonas sp. Strains and Detection of Methanotrophs during In Situ Bioremediation


  • A Novel process for Nitrogen Management in Bioreactor Landfills
  • Determination of mRNA of Methane Monooxygenase in Methylocystis sp. M
  • Improved System for Protein Engineering of the Hydroxylase Component of Soluble Methane Monooxygenase
  • Methane monooxygenase gene expression mediated by methanobactin in the presence of mineral copper sources
  • Microbial monooxygenases
  • Methane monooxygenase and its related biomimetic models


  • Consultant in Minnesota
  • Professor Consultant
  • Consultant in Washington
  • Consultant in Australia
  • Consultant in Massachusetts

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