Protein-derived cofactors. Expanding the scope of post-translational modifications.
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Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneMechanisms for control of biological electron transfer reactionsUnusual Chromophore and Cross-Links in Ranasmurfin: A Blue Protein from the Foam Nests of a Tropical FrogIn Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase ComplexFunctional Importance of Tyrosine 294 and the Catalytic Selectivity for the Bis-Fe(IV) State of MauG Revealed by Replacement of This Axial Heme Ligand with Histidine,Proline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauGCarboxyl Group of Glu113 Is Required for Stabilization of the Diferrous and Bis-Fe IV States of MauGThe precursor form ofHansenula polymorphacopper amine oxidase 1 in complex with CuIand CoIISite-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauGRoles of Conserved Residues of the Glycine Oxidase GoxA in Controlling Activity, Cooperativity, Subunit Composition, and Cysteine Tryptophylquinone Biosynthesis.Analytical Methods for Assessing the Effects of Site-Directed Mutagenesis on Protein-Cofactor and Protein-Protein Functional Relationships.Identifying proteins that can form tyrosine-cysteine crosslinks.Site selective reading of epigenetic markers by a dual-mode synthetic receptor array.Distribution in microbial genomes of genes similar to lodA and goxA which encode a novel family of quinoproteins with amino acid oxidase activity.A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.Roles of active site residues in LodA, a cysteine tryptophylquinone dependent ε-lysine oxidaseRoles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.A survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates: implications for ROS production, cancer etiology, and neurodegenerative diseases.MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.Interaction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis.Generation of protein-derived redox cofactors by posttranslational modification.Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.Activation of dioxygen by copper metalloproteins and insights from model complexes.Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity.Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesisIdentification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity.Suicide inactivation of MauG during reaction with O(2) or H(2)O(2) in the absence of its natural protein substrate.The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis.Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands.Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys-Tyr Cross-Link in the Galactose 6-Oxidase Homologue GlxA.Experimental and Theoretical Reduction Potentials of Some Biologically Active ortho-Carbonyl para-Quinones.Metals and Methanotrophy.Roles of Copper and a Conserved Aspartic Acid in the Autocatalytic Hydroxylation of a Specific Tryptophan Residue during Cysteine Tryptophylquinone Biogenesis.Structure and enzymatic properties of an unusual cysteine tryptophylquinone-dependent glycine oxidase from Pseudoalteromonas luteoviolacea.Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys-Tyr Cross-Link in the Galactose 6-Oxidase Homologue GlxA
P2860
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P2860
Protein-derived cofactors. Expanding the scope of post-translational modifications.
description
2007 nî lūn-bûn
@nan
2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Protein-derived cofactors. Expanding the scope of post-translational modifications.
@ast
Protein-derived cofactors. Expanding the scope of post-translational modifications.
@en
type
label
Protein-derived cofactors. Expanding the scope of post-translational modifications.
@ast
Protein-derived cofactors. Expanding the scope of post-translational modifications.
@en
prefLabel
Protein-derived cofactors. Expanding the scope of post-translational modifications.
@ast
Protein-derived cofactors. Expanding the scope of post-translational modifications.
@en
P356
P1433
P1476
Protein-derived cofactors. Expanding the scope of post-translational modifications.
@en
P2093
Victor L Davidson
P304
P356
10.1021/BI700468T
P407
P577
2007-04-17T00:00:00Z