MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

about

Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography.Heme enzyme structure and function.Genome mining for methanobactins Metals and Methanotrophy.

P2860

Q27303513-671BF8BB-17F3-4A03-94DC-B5D233D3E642 Q34396417-FDAD9259-3704-4667-B11A-73405554CB20 Q34601412-91F4DA0B-B697-43DE-B631-14603FA4F0A4 Q47197732-0B9ED876-F14F-4838-B318-797D9A399783

P2860

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

Item

http://www.wikidata.org/entity/Q36592463

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

@ast

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

@en

type

Item

label

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

@ast

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

@en

prefLabel

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

@ast

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

@en

P1476

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

@en

P2093

Carrie M Wilmot

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

P2860

Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases

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

Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa

Tryptophan-accelerated electron flow through proteins

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,

Nature of the Ferryl Heme in Compounds I and II

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

P304

3127-3135

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

P31

scholarly article

P356

10.1039/C2DT32059B

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

P407

English

P433

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

P478

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

P50

Erik Yukl

P577

2012-10-22T00:00:00Z

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

P698

23086017

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

P932

3566329

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

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

about

P2860

P2860

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932