Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii.

about

Structures of protein–protein complexes involved in electron transfer

P2860

Q27677090-99295499-28C8-42D6-AFE3-07BECCB3B91F

P2860

Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii.

Item

http://www.wikidata.org/entity/Q44448467

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh-hant

name

Characterization of a novel co ...... tase from Ralstonia pickettii.

@en

Characterization of a novel co ...... tase from Ralstonia pickettii.

@nl

type

Item

label

Characterization of a novel co ...... tase from Ralstonia pickettii.

@en

Characterization of a novel co ...... tase from Ralstonia pickettii.

@nl

prefLabel

Characterization of a novel co ...... tase from Ralstonia pickettii.

@en

Characterization of a novel co ...... tase from Ralstonia pickettii.

@nl

P1476

Characterization of a novel co ...... ctase from Ralstonia pickettii

@en

P2093

Cong Han

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

Karl Fisher

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

Robert R Eady

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

S Samar Hasnain

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

Stephen E J Rigby

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

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

pH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductase

Structure and function of a hexameric copper-containing nitrite reductase

The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted

Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications

X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner

Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 A resolution: comparison of blue and green nitrite reductases

Protein production by auto-induction in high density shaking cultures

Improved prediction of signal peptides: SignalP 3.0

ESPript: analysis of multiple sequence alignments in PostScript

P304

219-226

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

P31

scholarly article

P356

10.1042/BJ20111623

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

P407

English

P433

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

P478

444

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

P50

Gareth S A Wright

P577

2012-06-01T00:00:00Z

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

P698

22414182

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

Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii.

about

P2860

P2860

Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698