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Structure and Ligand Binding Properties of the Epoxidase Component of Styrene Monooxygenase,
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Production of enantiopure styrene oxide by recombinantEscherichia coli synthesizing a two-component styrene monooxygenase
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Integrated Biocatalytic Synthesis on Gram Scale: The Highly Enantioselective Preparation of Chiral Oxiranes with Styrene Monooxygenase
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Cloning, Heterologous Expression, and Enzymological Characterization of Human Squalene Monooxygenase
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FAD is a further essential cofactor of the NAD(P)H and O2‐dependent zeaxanthin‐epoxidase
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Crystal structure of p-hydroxybenzoate hydroxylase
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Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution
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Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase
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Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase
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Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases
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Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
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Crystal Structure of 3-Hydroxybenzoate Hydroxylase from Comamonas testosteroni Has a Large Tunnel for Substrate and Oxygen Access to the Active Site
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Phe161 and Arg166 variants of p‐hydroxybenzoate hydroxylase
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Activation of molecular oxygen by flavins and flavoproteins.
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[20] Processing of X-ray diffraction data collected in oscillation mode
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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
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The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
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Protein Dynamics Control Proton Transfers to the Substrate on the His72Asn Mutant of p-Hydroxybenzoate Hydroxylase
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Studies of the Mechanism of Phenol Hydroxylase: Mutants Tyr289Phe, Asp54Asn, and Arg281Met
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Complex Formation between Vibrio harveyi Luciferase and Monomeric NADPH:FMN Oxidoreductase
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Coordinated Production and Utilization of FADH 2 by NAD(P)H−Flavin Oxidoreductase and 4-Hydroxyphenylacetate 3-Monooxygenase
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Kinetics of a Two-Component p-Hydroxyphenylacetate Hydroxylase Explain How Reduced Flavin Is Transferred from the Reductase to the Oxygenase
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Stereospecific Biocatalytic Epoxidation: The First Example of Direct Regeneration of a FAD-Dependent Monooxygenase for Catalysis
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Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase
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Structure of the monooxygenase component of a two-component flavoprotein monooxygenase
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Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC
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Two Lysine Residues in the Bacterial Luciferase Mobile Loop Stabilize Reaction Intermediates
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Crystal Structure of the Oxygenase Component (HpaB) of the 4-Hydroxyphenylacetate 3-Monooxygenase from Thermus thermophilus HB8
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Searching protein structure databases with DaliLite v.3
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CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
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Structure and mechanism of para‐hydroxybenzoate hydroxylase
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Phaser crystallographic software
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PROCHECK: a program to check the stereochemical quality of protein structures
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The asymptotic leading term of anisotropic small-angle scattering intensities. II. Non-convex particles
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The 'Buccaneer' software for automated protein chain tracing
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The Mobile Flavin of 4-OH Benzoate Hydroxylase
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Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase
inferredcites →https://doi.org/10.1128/aem.59.10.3502-3504.1993openalex-snapshot
Adaptation of Pseudomonas putida S12 to high concentrations of styrene and other organic solvents
inferredcites →https://doi.org/10.1128/aem.64.6.2032-2043.1998openalex-snapshot
Towards a Biocatalyst for ( S )-Styrene Oxide Production: Characterization of the Styrene Degradation Pathway of Pseudomonas sp. Strain VLB120
inferredcites →https://doi.org/10.1128/jb.00966-06openalex-snapshot
Detection of Protein-Protein Interactions in the Alkanesulfonate Monooxygenase System from Escherichia coli
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Functional Analysis of the Small Component of the 4-Hydroxyphenylacetate 3-Monooxygenase ofEscherichia coliW: a Prototype of a New Flavin:NAD(P)H Reductase Subfamily
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Biochemical Characterization of StyAB from Pseudomonas sp. Strain VLB120 as a Two-Component Flavin-Diffusible Monooxygenase
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Automated Structure Solution With autoSHARP
inferredcites →https://doi.org/10.1529/biophysj.106.088633openalex-snapshot
Enantioselective Substrate Binding in a Monooxygenase Protein Model by Molecular Dynamics and Docking
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Structural and Mechanistic Insight into the Enantioselectivity of ( R )‐Selective Styrene Monooxygenases: A Tug‐of‐War between Proximal and Distal Residues
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