Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

@article{Lieberman2005CrystalSO,
  title={Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane},
  author={Raquel L. Lieberman and Amy C. Rosenzweig},
  journal={Nature},
  year={2005},
  volume={434},
  pages={177-182}
}
Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that catalyses the conversion of methane to methanol. Knowledge of how pMMO performs this extremely challenging chemistry may have an impact on the use of methane as an alternative energy source by facilitating the development of new synthetic catalysts. We have determined the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 Å. The enzyme is a trimer with an α3β3γ3… Expand
The quest for the particulate methane monooxygenase active site.
TLDR
The state of knowledge before and after the structure determination of pMMO is reviewed, emphasizing elucidation of the pM MO active site. Expand
Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).
TLDR
The authors briefly review the current understanding of the pMMO metal sites and discuss advances in small molecule Cu-O(2) chemistry that may contribute to an understanding of copper-ion mediated hydrocarbon oxidation chemistry. Expand
Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily
TLDR
The crystal structure of the corresponding domain of an archaeal amoB subunit from Nitrosocaldus yellowstonii has been determined and reveals a remarkable conservation of overall fold and copper binding site location as well as several notable differences that may have implications for function and stability. Expand
Architecture and active site of particulate methane monooxygenase
TLDR
Biochemical and spectroscopic data on pMMO and recombinant soluble fragments, denoted spmoB proteins, indicate that the active site involves copper and is located at the site of the dicopper center in the pmoB subunit. Expand
Controlled oxidation of hydrocarbons by the membrane-bound methane monooxygenase: the case for a tricopper cluster.
TLDR
Evidence is described that pMMO is a multicopper protein that mediates dioxygen chemistry and O-atom transfer during alkane hydroxylation and designed and synthesized model tricopper clusters to provide further chemical evidence that a tricoppers cluster mediates the enzyme's oxo-transfer chemistry. Expand
The model structure of the copper-dependent ammonia monooxygenase
TLDR
A successful attempt to build a structural model of ammonia monooxygenase, and its accessory proteins AmoD and AmoE, from Nitrosomonas europaea, taking advantage of the high sequence similarity with particulate methane mono oxygengenase and the homologous PmoD protein, for which crystal structures are instead available. Expand
Particulate Methane Monooxygenase
Particulate methane monooxygenase (pMMO) catalyzes the oxidation of methane to methanol in methanotrophic bacteria. The 300-kDa pMMO enzyme is a trimeric integral membrane protein, comprising threeExpand
From micelles to bicelles: Effect of the membrane on particulate methane monooxygenase activity
TLDR
These findings suggest that loss of pMMO activity upon isolation is due to removal from the membranes rather than caused by loss of the catalytic copper ions, and underscore the importance of studying membrane proteins in a membrane-like environment. Expand
A tale of two methane monooxygenases
TLDR
The current state of knowledge for both enzymes is reviewed, and pMMO O2 activation intermediates suggested by computational and synthetic studies in the context of existing biochemical data are considered. Expand
Evidence for oxygen binding at the active site of particulate methane monooxygenase.
TLDR
The reactivity of pMMO and spmoB with oxidants is investigated and strong new support for the identity and location of the pM MO active site is provided. Expand
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