- 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
Properties
- 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
Patent
- 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
Project
- 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)
Application
- 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)
|
Processing
- 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
Enzyme
- 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
Reports
- 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
Consultants
- Consultant in
Minnesota
- Professor
Consultant
- Consultant in
Washington
- Consultant in
Australia
- Consultant in
Massachusetts
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