Intermediate P* from soluble methane monooxygenase contains a diferrous cluster. - Wikidata - awgldk - TriplyDB

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

http://www.wikidata.org/entity/Q43089844

about

Enzymatic oxidation of methane Life in a sea of oxygen.Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system.Biocatalysts for methane conversion: big progress on breaking a small substrate.Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive.Structure of the key species in the enzymatic oxidation of methane to methanol Single Turnover Reveals Oxygenated Intermediates in Toluene/o-Xylene Monooxygenase in the Presence of the Native Redox Partners Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes.Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.A tale of two methane monooxygenases.Time-Resolved Investigations of Heterobimetallic Cofactor Assembly in R2lox Reveal Distinct Mn/Fe Intermediates.Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway.An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway.A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase.Spectroscopy and DFT Calculations of a Flavo-diiron Enzyme Implicate New Diiron Site Structures.Potential for cometabolic biodegradation of 1,4-dioxane in aquifers with methane or ethane as primary substrates.Diiron monooxygenases in natural product biosynthesis.

P2860

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P2860

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

http://www.wikidata.org/entity/Q43089844

description

2013 nî lūn-bûn

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2013年学术文章

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2013年学术文章

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name

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

@en

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

@nl

type

label

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

@en

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

@nl

prefLabel

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

@en

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

@nl

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P1476

Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.

@en

P2093

Eckard Münck

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

Katlyn K Meier

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

P2860

Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites

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

Probing the Function of Heme Distortion in the H-NOX Family

Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site

Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding

Revisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway.

Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.

Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme.

Mechanistic studies on the hydroxylation of methane by methane monooxygenase.

Methanotrophic bacteria.

P304

4331-4342

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scholarly article

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10.1021/BI400182Y

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25

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52

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John D. Lipscomb

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2013-06-13T00:00:00Z

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23718184

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3712755

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