Biological Methane Oxidation: Regulation, Biochemistry, and Active Site Structure of Particulate Methane Monooxygenase

@article{Lieberman2004BiologicalMO,
  title={Biological Methane Oxidation: Regulation, Biochemistry, and Active Site Structure of Particulate Methane Monooxygenase},
  author={Raquel L. Lieberman and Amy C. Rosenzweig},
  journal={Critical Reviews in Biochemistry and Molecular Biology},
  year={2004},
  volume={39},
  pages={147 - 164}
}
Particulate methane monooxygenase (pMMO) is a threesubunit integral membrane enzyme that catalyzes the oxidation of methane to methanol. Although pMMO is the predominant methane oxidation catalyst in nature, it has proved difficult to isolate, and most questions regarding its molecular structure, active site composition, chemical mechanism, and genetic regulation remain unanswered. Copper ions are believed to play a key role in both pMMO regulation and catalysis, and there is some evidence that… Expand
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Methane monooxygenase: functionalizing methane at iron and copper.
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Current understanding of the sMMO and pMMO protein structures, their methods for substrate channeling, and mechanisms for the dimetallic activation of O₂and C-H bonds are examined. Expand
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References

SHOWING 1-10 OF 133 REFERENCES
Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster
TLDR
Extended x-ray absorption fine structure data are best fit with oxygen/nitrogen ligands and a 2.57-Å Cu-Cu interaction, providing direct evidence for a copper-containing cluster in pMMO. Expand
Evidence that copper is a required cofactor for the membrane-bound form of methane monooxygenase
Abstract The membrane bound enzyme methane monooxygenase (pMMO) is a mixed function oxygenase that initiates the oxidative metabolism of methane in methanotrophic bacteria. In this paper, we showExpand
Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins.
TLDR
Different aspects of catalysis by the MMO proteins are examined, including the mechanisms of dioxygen activation at the diiron site and substrate hydroxylation by the activated oxygen species. Expand
The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath
TLDR
It is demonstrated that copper not only regulates the metabolic switch between the two methane monooxygenases but also regulates the level of expression of the pMMO and the development of internal membranes. Expand
The role of copper in the pMMO of Methylococcus capsulatus bath: a structural vs. catalytic function.
TLDR
The EPR spectra of the membrane fraction of Methylococcus capsulatus Bath are correlated with the amount of copper present in the membranes and to the activity of the pMMO as measured by the production of propylene oxide from propene by the pPMMO. Expand
The Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath) Is a Novel Copper-containing Three-subunit Enzyme
The particulate methane monooxygenase (pMMO) is known to be very difficult to study mainly due to its unusual activity instability in vitro. By cultivatingMethylococcus capsulatus (Bath) underExpand
Copper stress underlies the fundamental change in intracellular location of methane mono-oxygenase in methane-oxidizing organisms: Studies in batch and continuous cultures
SummaryThe intracellular location of methane mono-oxygenase (MMO) activity in the methanotroph Methylococcus capsulatus (Bath) has been shown to depend primarily on the availability of copper. MMOExpand
Biochemistry of the soluble methane monooxygenase.
TLDR
These roles appear to be related to regulation of catalysis, and are mediated by the formation of specific component complexes that alter the physical and catalytic properties of MMOH at different stages of the turnover cycle. Expand
Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath)
TLDR
DNA sequence analysis suggests that the primary structures of the β and γ subunit of MMO are completely novel and the complete sequence of these genes is presented. Expand
Regulation of bacterial methane oxidation: transcription of the soluble methane mono-oxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions.
TLDR
It was shown that the six ORFs of the sMMO gene cluster are organized as an operon and the transcripts produced upon expression of this operon have been identified and the synthesis of these transcripts was under control of a single copper-regulated promoter, which is as yet not precisely defined. Expand
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