Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone - Wikidata - awgldk - TriplyDB

Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone

Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone

http://www.wikidata.org/entity/Q24563330

about

Electron flow through biological molecules: does hole hopping protect proteins from oxidative damage?Mechanisms for control of biological electron transfer reactions Carboxyl Group of Glu113 Is Required for Stabilization of the Diferrous and Bis-Fe IV States of MauG Site-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauG Photochemical tyrosine oxidation in the structurally well-defined α3Y protein: proton-coupled electron transfer and a long-lived tyrosine radical Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ Heme enzyme structure and function.A simple method to engineer a protein-derived redox cofactor for catalysis.Could tyrosine and tryptophan serve multiple roles in biological redox processes?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.Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.Interaction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis.Long-range electron tunneling.A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.Roles of Copper and a Conserved Aspartic Acid in the Autocatalytic Hydroxylation of a Specific Tryptophan Residue during Cysteine Tryptophylquinone Biogenesis.Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.

P2860

Q26780147-D3464E3A-F547-4794-A3D4-E7ABADA7EB4C Q26866918-B607102B-C561-429B-B7E4-1543C2296EB0 Q27679703-D1FA861F-9E3D-4577-9729-34D2E0725EC9 Q27681679-B660DE9C-333A-4F5C-BD78-FB0F123E3985 Q34330608-CC6373F1-08CF-4767-8849-B530EF8B9202 Q34392839-D9774E70-FD00-4DE9-90FE-C1AF0EEC49AD Q34396417-82CD1524-A685-4DA4-95C5-691B4FCC2CC6 Q34850243-AEB67079-F4EA-4B9E-B963-D40A0B4F82E1 Q35128387-C18FDD28-3469-4C34-AE08-DED01C6DDC7D Q35690451-EE61541B-B296-45A0-9A86-BA0433D4F063 Q36055561-BF23014A-655E-47F2-8D01-C15D30FB171A Q36882674-54060DA3-31F0-4DFA-B392-AAA1555BD708 Q36995376-815ED231-4D59-4B35-9E77-A3EB132A8DA0 Q37360946-9230D93C-BD59-4E84-AFE1-EAF7B01AD163 Q37701849-3FC6F3BF-6D6F-4260-AC10-A3CEE41E6A76 Q41990838-62C21832-2246-42A4-863E-0E551D751D31 Q46347082-E4271586-7A96-4EBB-8D0B-52E5D021F3DC Q47828523-08C819D5-C6FF-4EE0-B79E-16BACDC355FC Q48170764-44208D73-2242-4729-9AB2-9DC09B18F918

P2860

Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone

http://www.wikidata.org/entity/Q24563330

description

2013 nî lūn-bûn

@nan

2013 թուականին հրատարակուած գիտական յօդուած

@hyw

2013 թվականին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年学术文章

@wuu

2013年学术文章

@zh-cn

2013年学术文章

@zh-hans

2013年学术文章

@zh-my

2013年学术文章

@zh-sg

2013年學術文章

@yue

name

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@ast

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@en

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@en-gb

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@nl

type

label

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@ast

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@en

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@en-gb

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@nl

prefLabel

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@ast

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@en

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@en-gb

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@nl

P1433

Q24563330-ED965E86-90F5-42F3-9A5C-9769AEFF5942

P1476

Q24563330-F59ADAA4-C724-4688-BD30-E9A0CBF8AB5C

P2860

Q24563330-0C9A10F2-504A-4840-B1BC-1C6A014079CF

Q24563330-0DE0B49A-F363-4699-92FC-169D85E16A30

Q24563330-15E05844-CC95-4107-B9A0-16EEB51FF24B

Q24563330-1C81A671-789F-4689-BA66-E9BE986C3ADC

Q24563330-1DF88477-AC15-49A3-A10B-9AAB785A2E84

Q24563330-1E7CDBA2-2D34-46B1-BA36-C768BB6869A5

Q24563330-220A6D52-43D1-4F0E-9E5C-0A110D732320

Q24563330-29F2F189-55F6-4868-9BBF-68F7E7AC279D

Q24563330-2D4B1323-457D-49EF-AE89-13E00DA8F812

Q24563330-2F5830C2-8797-4334-8B2E-0A94D302C8D9

P304

Q24563330-F7502C0B-C164-4B34-8BAB-6A663E1D59C1

P31

Q24563330-F7215E1E-6463-48FC-AE39-2CE64549E152

P356

Q24563330-1886E4A1-FFF9-421B-BB59-25D019DB519F

P407

Q24563330-D9427C6E-2D65-4CF2-9FB3-2A81FEEF0DC8

P433

Q24563330-74E01D1A-66CE-45D2-A6E6-53B9D0104DEA

P478

Q24563330-2A60830B-610B-4947-BBA5-1DC5248C5356

P50

Q24563330-AAA15082-3149-4452-AAC4-D753CDE8190B

Q24563330-C66566D7-A804-4814-A570-DFE0094FAD8C

P577

Q24563330-FF772873-238D-4544-8276-EF9D39AD7155

P698

Q24563330-7A7281B4-6FE2-4D99-BCCF-B4ECC24ED2C4

P932

Q24563330-69F88952-DC52-4845-8654-40A5731FD0A9

P356

ANNUREV-BIOCHEM-051110-133601

P1433

Annual Review of Biochemistry

P1476

Posttranslational biosynthesis ...... r tryptophan tryptophylquinone

@en

P2860

Review: studies of ferric heme proteins with highly anisotropic/highly axial low spin (S = 1/2) electron paramagnetic resonance signals with bis-histidine and histidine-methionine axial iron coordination

Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges

Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking

In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex

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 Activation

Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis

Proline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauG

Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i

Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution

P304

531-50

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1146/ANNUREV-BIOCHEM-051110-133601

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

82

http://www.w3.org/2001/XMLSchema#string

P50

Victor L. Davidson

Carrie M Wilmot

P577

2013-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

23746262

http://www.w3.org/2001/XMLSchema#string

P932

4082410

http://www.w3.org/2001/XMLSchema#string