about
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneMechanisms for control of biological electron transfer reactionsAcoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography.Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyaninTracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometryA single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyaninDefining the Role of the Axial Ligand of the Type 1 Copper Site in Amicyanin by Replacement of Methionine with LeucineIn Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase ComplexA joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transferFunctional 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 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein−Protein InterfaceCrystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen ActivationMutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesisDiradical intermediate within the context of tryptophan tryptophylquinone biosynthesisProline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauGStructures of MauG in complex with quinol and quinone MADHCarboxyl Group of Glu113 Is Required for Stabilization of the Diferrous and Bis-Fe IV States of MauGSite-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauGThe sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper siteRefined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolutionMolecular basis for interprotein complex-dependent effects on the redox properties of amicyaninElectron transfer in quinoproteinsTyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: implications for predicting electron transfer pathways.Protein control of true, gated, and coupled electron transfer reactions.Involvement of a putative [Fe-S]-cluster-binding protein in the biogenesis of quinohemoprotein amine dehydrogenase.Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation.What controls the rates of interprotein electron-transfer reactions.Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin.Electron transfer reactions between aromatic amine dehydrogenase and azurin.A simple method to engineer a protein-derived redox cofactor for catalysis.Chemically gated electron transfer. A means of accelerating and regulating rates of biological electron transfer.Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55.Use of the amicyanin signal sequence for efficient periplasmic expression in E. coli of a human antibody light chain variable domainA 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.Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG.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.Structure and mechanism of tryptophylquinone enzymes.Geometric and electronic structures of the His-Fe(IV)=O and His-Fe(IV)-Tyr hemes of MauG.A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Victor L. Davidson
@ast
Victor L. Davidson
@en
Victor L. Davidson
@es
Victor L. Davidson
@sl
type
label
Victor L. Davidson
@ast
Victor L. Davidson
@en
Victor L. Davidson
@es
Victor L. Davidson
@sl
prefLabel
Victor L. Davidson
@ast
Victor L. Davidson
@en
Victor L. Davidson
@es
Victor L. Davidson
@sl
P106
P1153
7102002772
P21
P31
P496
0000-0002-1966-7302