A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.
about
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneMechanisms for control of biological electron transfer reactionsIn 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 MauGSite-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauGProbing Bis-FeIV MauG: Isolation of Highly Reactive Radical Intermediates.Cofactor biosynthesis through protein post-translational modification.Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQHeme enzyme structure and function.A simple method to engineer a protein-derived redox cofactor for catalysis.Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenaseProbing 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.Characterization of the free energy dependence of an interprotein electron transfer reaction by variation of pH and site-directed mutagenesis.Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transferTryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.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.Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.Oxidation of methane by an N-bridged high-valent diiron-oxo species: electronic structure implications on the reactivity.Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex.Fractional transfer of a free unpaired electron to overcome energy barriers in the formation of Fe(4+) from Fe(3+) during the core contraction of macrocycles: implication for heme distortion.Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis
P2860
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P2860
A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
A catalytic di-heme bis-Fe(IV) ...... an Fe(IV)=O porphyrin radical.
@ast
A catalytic di-heme bis-Fe(IV) ...... an Fe(IV)=O porphyrin radical.
@en
type
label
A catalytic di-heme bis-Fe(IV) ...... an Fe(IV)=O porphyrin radical.
@ast
A catalytic di-heme bis-Fe(IV) ...... an Fe(IV)=O porphyrin radical.
@en
prefLabel
A catalytic di-heme bis-Fe(IV) ...... an Fe(IV)=O porphyrin radical.
@ast
A catalytic di-heme bis-Fe(IV) ...... an Fe(IV)=O porphyrin radical.
@en
P2093
P2860
P50
P356
P1476
A catalytic di-heme bis-Fe(IV) ...... an Fe(IV)=O porphyrin radical.
@en
P2093
Sheeyong Lee
Xianghui Li
P2860
P304
P356
10.1073/PNAS.0801643105
P407
P577
2008-06-18T00:00:00Z