Control of substrate access to the active site in methane monooxygenase
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Anatomy of enzyme channelsStructure of a Dinuclear Iron Cluster-Containing β-Hydroxylase Active in Antibiotic BiosynthesisAldehyde Decarbonylases: Enigmatic Enzymes of Hydrocarbon BiosynthesisEnzymatic oxidation of methaneStructural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.Evolution of mitochondria reconstructed from the energy metabolism of living bacteriaA flexible glutamine regulates the catalytic activity of toluene o-xylene monooxygenase.Biocatalysts for methane conversion: big progress on breaking a small substrate.Component interactions and electron transfer in toluene/o-xylene monooxygenase.(19)F NMR study of ligand dynamics in carboxylate-bridged diiron(II) complexes supported by a macrocyclic ligand.Coupling Oxygen Consumption with Hydrocarbon Oxidation in Bacterial Multicomponent Monooxygenases.Dynamic DMF Binding in MOF-5 Enables the Formation of Metastable Cobalt-Substituted MOF-5 Analogues.Inhibited proton transfer enhances Au-catalyzed CO2-to-fuels selectivity.Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate.All the O2 Consumed by Thermus thermophilus Cytochrome ba3 Is Delivered to the Active Site through a Long, Open Hydrophobic Tunnel with Entrances within the Lipid Bilayer.Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.Diiron oxidation state control of substrate access to the active site of soluble methane monooxygenase mediated by the regulatory component.A tale of two methane monooxygenases.Hydroxylation of methane through component interactions in soluble methane monooxygenases.Structure/function correlations over binuclear non-heme iron active sitesMetalloenzymes: Put a ring on it.Reconstitution of active mycobacterial binuclear iron monooxygenase complex in Escherichia coliElectron transfer control in soluble methane monooxygenase.Methanobactin and MmoD work in concert to act as the 'copper-switch' in methanotrophs.Dinuclear Complexes Formed by Hydrogen Bonds: Synthesis, Structure and Magnetic and Electrochemical Properties.Mutagenesis and expression of methane monooxygenase to alter regioselectivity with aromatic substrates.Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.On Dioxygen and Substrate Access to Soluble Methane Monooxygenases: An all-Atom Molecular Dynamics Investigation in Water Solution.Biosynthetic approach to modeling and understanding metalloproteins using unnatural amino acids
P2860
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P2860
Control of substrate access to the active site in methane monooxygenase
description
2013 nî lūn-bûn
@nan
2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Control of substrate access to the active site in methane monooxygenase
@ast
Control of substrate access to the active site in methane monooxygenase
@en
Control of substrate access to the active site in methane monooxygenase
@nl
type
label
Control of substrate access to the active site in methane monooxygenase
@ast
Control of substrate access to the active site in methane monooxygenase
@en
Control of substrate access to the active site in methane monooxygenase
@nl
prefLabel
Control of substrate access to the active site in methane monooxygenase
@ast
Control of substrate access to the active site in methane monooxygenase
@en
Control of substrate access to the active site in methane monooxygenase
@nl
P2093
P2860
P356
P1433
P1476
Control of substrate access to the active site in methane monooxygenase
@en
P2093
Michael S McCormick
Seung Jae Lee
Stephen J Lippard
Uhn-Soo Cho
P2860
P2888
P356
10.1038/NATURE11880
P407
P577
2013-02-21T00:00:00Z
P5875
P6179
1044352267