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Control of substrate access to the active site in methane monooxygenase

Control of substrate access to the active site in methane monooxygenase

http://www.wikidata.org/entity/Q27676275

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Anatomy of enzyme channels Structure of a Dinuclear Iron Cluster-Containing β-Hydroxylase Active in Antibiotic Biosynthesis Aldehyde Decarbonylases: Enigmatic Enzymes of Hydrocarbon Biosynthesis Enzymatic oxidation of methane Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.Evolution of mitochondria reconstructed from the energy metabolism of living bacteria A 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 sites Metalloenzymes: Put a ring on it.Reconstitution of active mycobacterial binuclear iron monooxygenase complex in Escherichia coli Electron 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

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P2860

Control of substrate access to the active site in methane monooxygenase

http://www.wikidata.org/entity/Q27676275

description

2013 nî lūn-bûn

@nan

2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի փետրվարին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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type

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Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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Control of substrate access to the active site in methane monooxygenase

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Michael S McCormick

http://www.w3.org/2001/XMLSchema#string

Seung Jae Lee

http://www.w3.org/2001/XMLSchema#string

Stephen J Lippard

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Uhn-Soo Cho

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Structure of the soluble methane monooxygenase regulatory protein B

Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase

Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site

X-ray crystal structure of alcohol products bound at the active site of soluble methane monooxygenase hydroxylase

X-ray Structure of a Hydroxylase−Regulatory Protein Complex from a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas sp. OX1 Phenol Hydroxylase † , ‡

Structural consequences of effector protein complex formation in a diiron hydroxylase

Active Site Threonine Facilitates Proton Transfer during Dioxygen Activation at the Diiron Center of Toluene/ o -Xylene Monooxygenase Hydroxylase

Analysis of Substrate Access to Active Sites in Bacterial Multicomponent Monooxygenase Hydroxylases: X-ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase from Pseudomonas sp. OX1

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10.1038/NATURE11880

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