Methane monooxygenase and its related biomimetic models

Westerheide, Lars

doi:10.1016/s1367-5931(99)00081-2

Cited by 45 publications

(13 citation statements)

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“…A prominent example are the prototypic so-called dimetal-oxygen cofactors, which are found, for example, in ribonucleotide reductases (RNRs) 5 (1-3), methane monooxygenases (4,5), and in various other oxidases (6 -8). RNRs are essential for DNA synthesis in all organisms (9).…”

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confidence: 99%

Rapid X-ray Photoreduction of Dimetal-Oxygen Cofactors in Ribonucleotide Reductase

Sigfridsson

Chernev

Leidel

et al. 2013

Journal of Biological Chemistry

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Background: Typical FeFe and MnFe cofactors bind to numerous enzymes such as ribonucleotide reductases. Crystallographic data suggest x-ray photoreduction (XPR) effects. Results: Rapid XPR-induced cofactor changes were monitored using time-resolved x-ray absorption spectroscopy. Conclusion: The XPR-induced cofactor states differ significantly from the native configurations, but comply with crystallographic structures. Significance: Structure determination for high-valent dimetal-oxygen cofactors requires free electron-laser protein crystallography combined with x-ray spectroscopy.

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confidence: 99%

Rapid X-ray Photoreduction of Dimetal-Oxygen Cofactors in Ribonucleotide Reductase

Sigfridsson

Chernev

Leidel

et al. 2013

Journal of Biological Chemistry

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“…Converting natural gas into a liquid commodity chemical, methanol, would provide a crucial improvement in industrial practice and an opportunity to use stranded natural gas resources that are otherwise flared. We believe this reaction to be a particularly interesting choice for hybrid organic/inorganic catalysts, as researchers working on this transformation have been often inspired by methane monooxygenase enzymes (MMO), hybrid biological catalysts which can turn methane into methanol at room temperature and ambient pressure in the presence of molecular oxygen. , The enzyme contains metal ions in its active site (low nuclearity Cu and Fe sites) to perform O 2 activation and C–H bond scission. Local ligand environments dictated by amino acid residues form reactive electrophilic metal–oxygen species.…”

Section: On the Design Of Hybrid Catalysts For Methane-to-methanol Tr...mentioning

confidence: 99%

Design of Organic/Inorganic Hybrid Catalysts for Energy and Environmental Applications

2020

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Controlling selectivity between competing reaction pathways is crucial in catalysis. Several approaches have been proposed to achieve this goal in traditional heterogeneous catalysts including tuning nanoparticle size, varying alloy composition, and controlling supporting material. A less explored and promising research area to control reaction selectivity is via the use of hybrid organic/inorganic catalysts. These materials contain inorganic components which serve as sites for chemical reactions and organic components which either provide diffusional control or directly participate in the formation of active site motifs. Despite the appealing potential of these hybrid materials to increase reaction selectivity, there are significant challenges to the rational design of such hybrid nanostructures. Structural and mechanistic characterization of these materials play a key role in understanding and, therefore, designing these organic/inorganic hybrid catalysts. This Outlook highlights the design of hybrid organic/inorganic catalysts with a brief overview of four different classes of materials and discusses the practical catalytic properties and opportunities emerging from such designs in the area of energy and environmental transformations. Key structural and mechanistic characterization studies are identified to provide fundamental insight into the atomic structure and catalytic behavior of hybrid organic/inorganic catalysts. Exemplary works are used to show how specific active site motifs allow for remarkable changes in the reaction selectivity. Finally, to demonstrate the potential of hybrid catalyst materials, we suggest a characterization-based approach toward the design of biomimetic hybrid organic/inorganic materials for a specific application in the energy and environmental research space: the conversion of methane into methanol.

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“…They exist in a lot of organisms. Nucleotide sequence analysis of the tetrahydrofuran monooxygenase showed that this monooxygenase was special to other monooxygenases in sequence similarity, though its encoding peptide contained the four highly conserved glutamate residues and two histidine residues which might be involved in coordination of the active-site binuclear-iron center (Westerheide et al, 2000). The specificity of these monooxygenase genes were further experimentally verified by PCR amplification using genespecial primers.…”

Section: Sequence Specificity Of the Tetrahydrofuran Monooxygenase Genesmentioning

confidence: 99%

Evidence for horizontal gene transfer of a tetrahydrofuran monooxygenase: Cloning and analysis of a gene cluster for tetrahydrofuran degradation in Rhodococcus sp. YYL

Yao¹,

Lü²,

Zhu³

et al. 2013

Afr. J. Microbiol. Res.

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A gene cluster encoding tetrahydrofuran (THF) degrading related enzymes was first isolated from Rhodococcus sp. YYL, a strain of the genus Rhodococcus, which was first reported to degrade tetrahydrofuran, by combination of COnsensus-DEgenerate Hybrid oligonucleotide Primer PCR and thermal asymmetric interlaced PCR. Sequence analysis of the gene cluster revealed 9 open reading frames containing genes encoding a Rhodococcus sp. YYL multiple component tetrahydrofuran monooxygenase. The tetrahydrofuran monooxygenase genes had similarities higher than 92% with these in Pseudonocardia sp. K1, but had low similarities with other monooxygenase genes using BLAST search in GenBanK. The high specific of tetrahydrofuran monooxygenase genes was further proved by PCR amplification of no product using genomic DNA of other bacteria or even activated sludge as template with primers targeting at the α-subunit of this monooxygenase. Phylogenetic analysis based on amino acid sequences and 16S rDNA strongly suggested that this monooxygenase occurred by horizontal gene transfer. Base composition analysis and the existence of a transposase gene in the gene cluster further proposed that this monooxygenase originated from the genus Rhodococcus and it might be transformed by a transposon between different species.

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Methane monooxygenase and its related biomimetic models

Cited by 45 publications

References 44 publications

Rapid X-ray Photoreduction of Dimetal-Oxygen Cofactors in Ribonucleotide Reductase

Rapid X-ray Photoreduction of Dimetal-Oxygen Cofactors in Ribonucleotide Reductase

Design of Organic/Inorganic Hybrid Catalysts for Energy and Environmental Applications

Evidence for horizontal gene transfer of a tetrahydrofuran monooxygenase: Cloning and analysis of a gene cluster for tetrahydrofuran degradation in Rhodococcus sp. YYL

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