Proline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauG
about
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneCarboxyl 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-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.Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.Tryptophan-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 biosynthesisOxidative 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.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.On the pathways of biologically relevant diatomic gases through proteins. Dioxygen and heme oxygenase from the perspective of molecular dynamics.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.A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Gates and binding pockets for nitric oxide with cytochrome c', according to molecular dynamics.Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.
P2860
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P2860
Proline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauG
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2012 nî lūn-bûn
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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2012 թվականի փետրվարին հրատարակված գիտական հոդված
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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name
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@ast
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@en
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@en-gb
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@nl
type
label
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@ast
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@en
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@en-gb
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@nl
prefLabel
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@ast
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@en
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@en-gb
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@nl
P2093
P2860
P50
P356
P1433
P1476
Proline 107 Is a Major Determi ...... of the High-Spin Heme of MauG
@en
P2093
Lyndal M R Jensen
Manliang Feng
Xiaoxi Wei
P2860
P304
P356
10.1021/BI201882E
P407
P577
2012-02-28T00:00:00Z