The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

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Small electron-transfer proteins as mediators in enzymatic electrochemical biosensors.

P2860

Q46682597-AEC737C0-2EDF-4484-8542-EC7F58FB4E25

P2860

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

Item

http://www.wikidata.org/entity/Q46095634

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh-hant

name

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

@en

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

@nl

type

Item

label

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

@en

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

@nl

prefLabel

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

@en

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

@nl

P1476

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

@en

P2093

Kenji Kano

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

Megumi Mori

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

Nobutaka Fujieda

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

Tokuji Ikeda

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

P2860

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

Involvement of a putative [Fe-S]-cluster-binding protein in the biogenesis of quinohemoprotein amine dehydrogenase.

Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation.

Mechanism of post-translational quinone formation in copper amine oxidases and its relationship to the catalytic turnover.

Emerging principles of inorganic nitrogen metabolism in Paracoccus denitrificans and related bacteria.

Novel principles in the microbial conversion of nitrogen compounds.

Mutational analysis of mau genes involved in methylamine metabolism in Paracoccus denitrificans.

Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins.

Spectroelectrochemical evaluation of redox potentials of cysteine tryptophylquinone and two hemes c in quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

P304

524-529

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

P31

scholarly article

P356

10.1271/BBB.80578

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

P433

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

P478

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

P577

2009-03-07T00:00:00Z

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

P698

19270386

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

P921

Paracoccus denitrificans

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

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P2860

P2860

The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921