The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath).

Nguyen, H.-Hoa T.; Shiemke, Andrew K.; Jacobs, Sheila J.; Hales, Brian J.; Lidstrom, Mary E.; Chan, Sunney I.

doi:10.1016/s0021-9258(17)36565-1

Cited by 190 publications

(101 citation statements)

References 20 publications

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“…NMR spectra were recorded with Bruker AV400 ( 1 H 400.1 MHz, 13 C 100.6 MHz, 31 P 162.0 MHz), AV 500 ( 1 H 500.1 MHz, 13 C 125.8 MHz), and AV600 ( 31 P 242.8 MHz) NMR spectrometers in CD 2 Cl 2 and CDCl 3 at 25 °C if not reported differently. 1 H NMR spectra were calibrated against the internal residual proton and natural abundance 13 C resonances of the deuterated solvent. Chemical shifts (δ) were reported in ppm, coupling constants (J) in Hz.…”

Section: Methodsmentioning

confidence: 99%

“…The resulting solid was recrystallized from diethyl ether and diphenylbis(3phenyl-1H-pyrazol-1-yl)methane was collected as a colourless solid in poor yield (194 mg, 0.43 mmol, 28 %). 1 [Cu PhPh Bpm(MeCN)]BF 4 (4). To a solution of di(3-(phenyl)-1Hpyrazol-1-yl)diphenylmethane (100 mg, 0.22 mmol, 1 eq) in dichloromethane (5 mL) a solution of tetrakis(acetonitrile)copper(I) tetrafluoroborate (77 mg, 0.24 mmol, 1.1 eq) in acetonitrile (5 mL) was added.…”

Section: Di(3-(phenyl)-1h-pyrazol-1-yl)diphenylmethane Phphmentioning

confidence: 99%

“…For a long time, the constitution and structure of the particulate methanemonooxygenase (pMMO), which catalyses the synthetically challenging oxygenation of methane to methanol, has been a subject of controversial discussions. [1][2][3][4][5][6][7][8][9] However, within recent years combined crystallographic, biochemical and quantum mechanical investigations by Rosenzweig and coworkers have revealed that the enzyme contains three mononuclear copper site, [10] two of which, Cu B and Cu C , have been discussed in recent years as the active, methane-oxidizing centres. [10,14] While currently Cu C is proposed as the active site, Cu B is essential, too.…”

Section: Introductionmentioning

confidence: 99%

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Mimicking of the histidine brace structural motif in molecular copper(I) compounds

Peifer

Müller

Hoof

et al. 2021

Zeitschrift anorg allge chemie

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Dedicated to Professor Hansgeorg Schnöckel on occasion of his 80 th birthday L-Nτ-methylhistidine methyl ester, MeHisOMe, has been employed as a potential ligand to mimic the histidine brace-type coordination of copper ions in enzymes such as the particulate methane monoxygenase or lytic polysaccharide monooxygenases. MeHisOMe was prepared by double-methylation of histidine methyl ester. Subsequently, its complexation by diphosphine copper(I) precursors [Cu(P^P)(MeCN) 2 ]BF 4 was tested, which led to the complexes [Cu(P^P)(MeHisOMe)]BF 4 (P^P = dpePhos: 1, P^P = XantPhos: 2, P^P = dppf: 3). 1-3 were fully characterized, also by single crystal X-ray analysis, thus providing first structural data for copper complexes with a synthetic, authentic histidine brace. The complexes proved inert in contact with dioxygen. To improve the biomimetic character attempts were made to formally replace the diphosphine ligands by bis(pyrazolyl)methanes, Bpm. Correspondingly, [BpmCu(NCMe) x ]BF 4 precursors were synthesized, with different substituents at the 3-positions of the pyrazolyl (i. e. Bpm = di(3-(phenyl)-1H-pyrazol-1-yl)diphenylmethane, di(3-(mesityl)-1Hpyrazol-1-yl)methane and di(3-(tert-butyl)-1H-pyrazol-1-yl) diphenylmethane). Addition of MeHisOMe to these complexes led to products that were so sensitive towards oxidation by the environment that they eluded isolation. One experiment provided blue crystals as a product of such a reaction. They belonged to a salt with a complex cation consisting of a Cu(μ-OH) 2 Cu core ligated by two MeHisOMe ligands, which dimerises in the solid state to give [Cu 4 (OH) 4 (MeHisOMe) 4 ] 4 + .

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Section: Methodsmentioning

confidence: 99%

Section: Di(3-(phenyl)-1h-pyrazol-1-yl)diphenylmethane Phphmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Mimicking of the histidine brace structural motif in molecular copper(I) compounds

Peifer

Müller

Hoof

et al. 2021

Zeitschrift anorg allge chemie

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“…Together with Drew, he carried out a detailed study of the effects of copper concentration on the methane monooxygenase activity of the membranes isolated from cells of M. capsulatus, and correlated the specific activity with the level of copper that was determined to be associated with these membranes. They concluded that the pMMO was indeed produced in high levels in the membranes when the bacterium was cultured at high copper concentration in the growth media, and that it was a multicopper protein containing as many as 15 copper ions per 100 kDa (71). From a quantitative proteomic analysis of bacterial cells obtained when the bacterium was grown under copper stress (48), we now know that copper ions are essential for the expression of the pMMO gene and growth of the organism.…”

Section: Particulate Methane Monooxygenase: a Membrane-bound Enzyme That Oxidizes Methane To Methanolmentioning

confidence: 99%

Untitled

2009

Annu. Rev. Biophys.

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“…Whereas pMMO is bound to the cell membrane, sMMO exists in the cytoplasm [15]. Both pMMO and sMMO require distinct metal elements as a prosthetic group (copper ions and iron ions, respectively) [16][17][18]. Methanol is oxidized to formaldehyde by methanol dehydrogenase [19].…”

Section: Introductionmentioning

confidence: 99%

Genomic and Physiological Properties of a Facultative Methane-Oxidizing Bacterial Strain of Methylocystis sp. from a Wetland

et al. 2020

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Methane-oxidizing bacteria are crucial players in controlling methane emissions. This study aimed to isolate and characterize a novel wetland methanotroph to reveal its role in the wetland environment based on genomic information. Based on phylogenomic analysis, the isolated strain, designated as B8, is a novel species in the genus Methylocystis. Strain B8 grew in a temperature range of 15 °C to 37 °C (optimum 30–35 °C) and a pH range of 6.5 to 10 (optimum 8.5–9). Methane, methanol, and acetate were used as carbon sources. Hydrogen was produced under oxygen-limited conditions. The assembled genome comprised of 3.39 Mbp and 59.9 mol% G + C content. The genome contained two types of particulate methane monooxygenases (pMMO) for low-affinity methane oxidation (pMMO1) and high-affinity methane oxidation (pMMO2). It was revealed that strain B8 might survive atmospheric methane concentration. Furthermore, the genome had various genes for hydrogenase, nitrogen fixation, polyhydroxybutyrate synthesis, and heavy metal resistance. This metabolic versatility of strain B8 might enable its survival in wetland environments.

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The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath).

Cited by 190 publications

References 20 publications

Mimicking of the histidine brace structural motif in molecular copper(I) compounds

Mimicking of the histidine brace structural motif in molecular copper(I) compounds

Untitled

Genomic and Physiological Properties of a Facultative Methane-Oxidizing Bacterial Strain of Methylocystis sp. from a Wetland

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