In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex
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.Functional 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 biosynthesisStructure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobicallyDiradical 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 MADHStructure of the processive rubber oxygenase RoxA from Xanthomonas spCarboxyl 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 MauGHigh-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of the identity of the protein and its potential role in detoxificationThe inner workings of the hydrazine synthase multiprotein complexProbing Bis-FeIV MauG: Isolation of Highly Reactive Radical Intermediates.Identifying proteins that can form tyrosine-cysteine crosslinks.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.Automated sample-scanning methods for radiation damage mitigation and diffraction-based centering of macromolecular crystals.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.Tuning of Hemes b Equilibrium Redox Potential Is Not Required for Cross-Membrane Electron Transfer.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.Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.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.Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways.Generation of protein-derived redox cofactors by posttranslational modification.Modularity of methylotrophy, revisited.Another look at the interaction between mitochondrial cytochrome c and flavocytochrome b (2).
P2860
Q24563330-8138F495-ACAB-4B37-8AAB-7946AEB624CDQ26866918-689C7E2E-425D-489B-892E-A3BEDD5EE12BQ27303513-095784E2-A084-46D2-9EC8-E30AD1CB9191Q27664940-D3D6F301-1E4B-4A0C-8469-99466469EC4CQ27667083-2DFFDED4-EF48-407B-8338-911518631C00Q27674714-1A7A0B84-0976-40BD-8D61-63D9812843DAQ27675848-F3EA382C-3579-4363-82E4-094DFFC4317BQ27676809-DC496069-80CC-4D10-B62F-7AF0010047BBQ27677014-865B05A0-426E-4E86-9A12-0C4EEDA2701EQ27678964-75350D29-6E8C-40D5-9D41-ED51DD945E91Q27679417-1DDB28A9-F603-4EC9-9CA6-3F63DB182DCFQ27679703-7B023482-451A-4B78-85D8-7D7540A95CD1Q27681679-53897649-D266-42CA-8FAD-6718752C81EAQ27682142-0ECE4220-2BE8-44B9-A268-40824023C549Q27702490-7A133D11-B4FB-4BF8-924C-5DC5529DE627Q30101088-015094A3-8C50-4788-94BC-EC65D940302BQ30419194-19A1C279-1906-42D7-B256-9B409CA6A87EQ34258394-D7692AC8-37FC-44F5-BAE2-7DB665710240Q34392839-11A96521-393E-4649-A56D-7CBCCB0AF878Q34396417-930B5C90-D866-4228-AD91-9B14C010CA60Q34850243-589CF724-D185-458A-AA22-672DE9780AC5Q35181324-8F984F56-467A-4402-AD45-40A05A45E416Q35188543-EDCEC7DC-58F7-47B5-958C-760D2789874AQ35690451-BD09EDCB-6F66-48A7-A281-4780DAF27F68Q35804440-BA56EC46-73A3-4434-A7A5-F20B63C5245DQ36055561-C603AE09-0DDD-40A0-AD21-D7CCACAB107EQ36428853-D4AEC509-9D75-4175-8AEF-D19A14F12701Q36592463-4AC85969-42DD-45DE-9A7D-0923F5F1B619Q36727394-97F9E7F2-5B75-4B0D-A99D-FB98CE592FFEQ36832368-2762F344-EA51-4FB5-9B98-B1584CADCA9BQ36882674-92F883F4-7D45-45E1-970E-9AB079646E10Q36932428-6C78CED7-E64B-4E42-B266-BB6B76B47B36Q36995376-F4C2DEAA-725A-44D2-B757-86DEECB59E2EQ37090935-0F469BA0-E18C-408A-B303-25F41968A656Q37104425-7F81767A-DD2D-47C8-BD62-EB6B6E1F778FQ37360946-2C520B1D-60D3-47CE-A37D-55D68C64A795Q37600547-0D19DE0B-045F-4430-8E7B-0EDE5865D2B3Q37799264-41353E47-F1E3-49D2-8B52-9E30A7FB2D91Q37858657-C8FE165E-A185-412A-9A70-401E0E319A7BQ37866680-31C6CEBC-F5E1-424A-8EEB-A513C665BB71
P2860
In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@ast
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@en
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@en-gb
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@nl
type
label
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@ast
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@en
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@en-gb
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@nl
prefLabel
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@ast
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@en
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@en-gb
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@nl
P2860
P356
P1433
P1476
In Crystallo Posttranslational ...... hylamine Dehydrogenase Complex
@en
P2093
Lyndal M R Jensen
Ruslan Sanishvili
P2860
P304
P356
10.1126/SCIENCE.1182492
P407
P577
2010-03-12T00:00:00Z