Mechanism of Aromatic Amino Acid Hydroxylation
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This article is published in Biochemistry.The article was published on 2003-12-09 and is currently open access. It has received 247 citations till now. The article focuses on the topics: Hydroxylation & Aromatic amino acids.read more
Citations
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Non-heme Fe(IV)-oxo intermediates.
TL;DR: The observation of non-heme Fe(IV)-oxo intermediates and Fe(II)-containing product(s) complexes with almost identical spectroscopic parameters in the reactions of two distantly related alphaKG-dependent hydroxylases suggests that members of this subfamily follow a conserved mechanism for substrate hydroxyation.
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Complexity of dopamine metabolism
TL;DR: This review highlights different aspects of dopamine metabolism in the context of PD and neurodegeneration by looking at DA biosynthesis, sequestration, degradation and oxidation chemistry at the metabolic level, as well as at the transcriptional, translational and posttranslational regulation of all enzymes involved.
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Synthetic models of the active site of catechol oxidase: mechanistic studies
TL;DR: This critical review extensively discusses the synthetic models of catechol oxidase, with a particular emphasis on the different approaches used in the literature to study the mechanism of the catalytic oxidation of the substrate (catechol) by these compounds.
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The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes.
TL;DR: In this paper, the authors summarize crystallographic and mechanistic features of this metalloenzyme superfamily, which has enabled the proposal of a common but flexible pathway for dioxygen activation.
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Tetrahydrobiopterin: biochemistry and pathophysiology.
TL;DR: A major contributor to vascular dysfunction associated with hypertension, ischaemic reperfusion injury, diabetes and others, appears to be an effect of oxidized BH4, which leads to an increased formation of oxygen-derived radicals instead of NO by decoupled NOS.
References
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Heme-Containing Oxygenases
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Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes
Edward I. Solomon,Thomas C. Brunold,Mindy I. Davis,Jyllian N. Kemsley,Sang-Kyu Lee,Nicolai Lehnert,Frank Neese,Andrew J. Skulan,Yi-Shan Yang,Jing Zhou +9 more
TL;DR: A detailed molecular mechanism has been proposed for IPNS based on spectroscopic and crystallographic studies and the role of cosubstrate ascorbate is proposed to reduce the toxic peroxo byproduct to water.
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Activation of molecular oxygen by flavins and flavoproteins.
TL;DR: Clearly the reactivity of the reduced flavin with 0, is modulated by the protein environment in which i t is located, both in terms of rates and products of the reaction.
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Crystallographic and spectroscopic characterization of a nonheme Fe(IV)-O complex.
Jan Uwe Rohde,Jun Hee In,Jun Hee In,Mi Hee Lim,Mi Hee Lim,William W. Brennessel,Michael R. Bukowski,Audria Stubna,Eckard Münck,Wonwoo Nam,Lawrence Que +10 more
TL;DR: High-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.
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Tetrahydropterin-dependent amino acid hydroxylases.
TL;DR: Reversible phosphorylation of serine residues in the regulatory domains affects the activities of all three enzymes, and phenylalanine hydroxylase is allosterically regulated by its substrates, phenylAlanine and tetrahydrobiopterin.