Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation.
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Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneMechanisms for control of biological electron transfer reactionsAn oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein MopEIn 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,Crystal 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 MauGCorA Is a Copper Repressible Surface-Associated Copper(I)-Binding Protein Produced in Methylomicrobium album BG8Site-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauGIdentifying proteins that can form tyrosine-cysteine crosslinks.Involvement of a putative [Fe-S]-cluster-binding protein in the biogenesis of quinohemoprotein amine dehydrogenase.Expansion of substrate specificity of cytochrome P450 2A6 by random and site-directed mutagenesis.Pyrroloquinoline quinone biogenesis: demonstration that PqqE from Klebsiella pneumoniae is a radical S-adenosyl-L-methionine enzyme.Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQA simple method to engineer a protein-derived redox cofactor for catalysis.Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.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.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 multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.Geometric and electronic structures of the His-Fe(IV)=O and His-Fe(IV)-Tyr hemes of MauG.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.A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesisUncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways.MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Generation of protein-derived redox cofactors by posttranslational modification.Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.Bis-Fe(IV): nature's sniper for long-range oxidation.Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex.Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesisA Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.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.Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase.
P2860
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P2860
Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation.
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2004 nî lūn-bûn
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2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Further insights into quinone ...... n tryptophylquinone formation.
@ast
Further insights into quinone ...... n tryptophylquinone formation.
@en
Further insights into quinone ...... n tryptophylquinone formation.
@en-gb
type
label
Further insights into quinone ...... n tryptophylquinone formation.
@ast
Further insights into quinone ...... n tryptophylquinone formation.
@en
Further insights into quinone ...... n tryptophylquinone formation.
@en-gb
prefLabel
Further insights into quinone ...... n tryptophylquinone formation.
@ast
Further insights into quinone ...... n tryptophylquinone formation.
@en
Further insights into quinone ...... n tryptophylquinone formation.
@en-gb
P2093
P50
P356
P1433
P1476
Further insights into quinone ...... n tryptophylquinone formation.
@en
P2093
Limei H Jones
M Elizabeth Graichen
Paul A Grimsrud
Sean A Agger
Sudha Marimanikkupam
Teresa De La Mora-Rey
Yongting Wang
P304
P356
10.1021/BI049863L
P407
P577
2004-05-01T00:00:00Z