Mössbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus bath: evidence for a Diiron center.
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Architecture and active site of particulate methane monooxygenaseThe Metal Centers of Particulate Methane Monooxygenase from Methylosinus trichosporium OB3bCrystal Structure and Characterization of Particulate Methane Monooxygenase from Methylocystis species Strain MEffects of Zinc on Particulate Methane Monooxygenase Activity and StructureMethanobactin transport machineryCopper active sites in biologyEnzymatic oxidation of methaneIdentification of the valence and coordination environment of the particulate methane monooxygenase copper centers by advanced EPR characterizationA comparison of methanobactins from Methylosinus trichosporium OB3b and Methylocystis strain Sb2 predicts methanobactins are synthesized from diverse peptide precursors modified to create a common core for binding and reducing copper ions.Oxidation of methane by a biological dicopper centreTranscription of nitrification genes by the methane-oxidizing bacterium, Methylococcus capsulatus strain Bath.A soluble form of ammonia monooxygenase in Nitrosomonas europaea.Dual pathways for copper uptake by methanotrophic bacteria.Trace metal requirements for microbial enzymes involved in the production and consumption of methane and nitrous oxide.Chemistry and biology of the copper chelator methanobactin.Evidence for oxygen binding at the active site of particulate methane monooxygenase.The metal centres of particulate methane mono-oxygenase.Methanobactin and the Link between Copper and Bacterial Methane OxidationCopper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.A tale of two methane monooxygenases.Alkane-oxidizing metalloenzymes in the carbon cycle.Methane oxidation by anaerobic archaea for conversion to liquid fuels.A TonB-Dependent Transporter Is Responsible for Methanobactin Uptake by Methylosinus trichosporium OB3bNMR, mass spectrometry and chemical evidence reveal a different chemical structure for methanobactin that contains oxazolone rings.Discrimination of the prochiral hydrogens at the C-2 position of n-alkanes by the methane/ammonia monooxygenase family proteins.Cage escape competes with geminate recombination during alkane hydroxylation by the diiron oxygenase AlkB.Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit.Detoxification of mercury by methanobactin from Methylosinus trichosporium OB3b.A radical rebound mechanism for the methane oxidation reaction promoted by the dicopper center of a pMMO enzyme: a computational perspective.Metals and Methanotrophy.Quantum Refinement Does Not Support Dinuclear Copper Sites in Crystal Structures of Particulate Methane Monooxygenase.Methanobactins: maintaining copper homeostasis in methanotrophs and beyond.57Fe Mössbauer Spectroscopy in Chemistry and Biology
P2860
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P2860
Mössbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus bath: evidence for a Diiron center.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Mössbauer studies of the membr ...... evidence for a Diiron center.
@en
Mössbauer studies of the membr ...... evidence for a Diiron center.
@nl
type
label
Mössbauer studies of the membr ...... evidence for a Diiron center.
@en
Mössbauer studies of the membr ...... evidence for a Diiron center.
@nl
prefLabel
Mössbauer studies of the membr ...... evidence for a Diiron center.
@en
Mössbauer studies of the membr ...... evidence for a Diiron center.
@nl
P2093
P2860
P356
P1476
Mössbauer studies of the membr ...... : evidence for a Diiron center
@en
P2093
Alan A Dispirito
Dong W Choi
Eckard Münck
William E Antholine
P2860
P304
15783-15785
P356
10.1021/JA077682B
P407
P577
2007-12-05T00:00:00Z