Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase.
about
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneMechanisms for control of biological electron transfer reactionsDefining 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 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 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein−Protein InterfaceMutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesisProline 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 MauGSite-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauGFunctional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.A simple method to engineer a protein-derived redox cofactor for catalysis.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.Determination of enzyme mechanisms by molecular dynamics: studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenaseA catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.Characterization of the free energy dependence of an interprotein electron transfer reaction by variation of pH and site-directed mutagenesis.A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesisInteraction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis.Mechanisms of ammonia activation and ammonium ion inhibition of quinoprotein methanol dehydrogenase: a computational approachMauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase.Generation of protein-derived redox cofactors by posttranslational modification.Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes.Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.Combining metagenomics with metaproteomics and stable isotope probing reveals metabolic pathways used by a naturally occurring marine methylotroph.Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex.Catalysis of Heterocyclic Azadiene Cycloaddition Reactions by Solvent Hydrogen Bonding: Concise Total Synthesis of Methoxatin.Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesisMethylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources.Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis.Correlation of rhombic distortion of the type 1 copper site of M98Q amicyanin with increased electron transfer reorganization energy.Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55.Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.Metals and Methanotrophy.
P2860
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P2860
Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Pyrroloquinoline quinone (PQQ) ...... rom methylamine dehydrogenase.
@ast
Pyrroloquinoline quinone (PQQ) ...... rom methylamine dehydrogenase.
@en
type
label
Pyrroloquinoline quinone (PQQ) ...... rom methylamine dehydrogenase.
@ast
Pyrroloquinoline quinone (PQQ) ...... rom methylamine dehydrogenase.
@en
prefLabel
Pyrroloquinoline quinone (PQQ) ...... rom methylamine dehydrogenase.
@ast
Pyrroloquinoline quinone (PQQ) ...... rom methylamine dehydrogenase.
@en
P1476
Pyrroloquinoline quinone (PQQ) ...... rom methylamine dehydrogenase.
@en
P2093
Davidson VL
P304
P356
10.1016/S0065-3233(01)58003-1
P577
2001-01-01T00:00:00Z