Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

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Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c'Heme and nitric oxide binding by the transcriptional regulator DnrF from the marine bacterium Dinoroseobacter shibae increases napD promoter affinity.

P2860

Q27701174-6C1846AE-4BF6-4433-B4E0-7DF076042F64 Q47814648-2FFA2A2B-7452-46AB-A196-EC9D82E554DF

P2860

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

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http://www.wikidata.org/entity/Q51069376

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2014 nî lūn-bûn

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2014年の論文

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2014年学术文章

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2014年学术文章

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@zh-hant

name

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

@en

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

@nl

type

Item

label

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

@en

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

@nl

prefLabel

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

@en

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

@nl

P1476

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR

@en

P2093

Francesca Cutruzzolà

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

Giorgio Giardina

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

Serena Rinaldo

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

Stefano della Longa

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

P2860

Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase

A Redox-controlled Molecular Switch Revealed by the Crystal Structure of a Bacterial Heme PAS Sensor

Structure-based hypothesis on the activation of the CO-sensing transcription factor CooA

An X-ray diffraction and X-ray absorption spectroscopy joint study of neuroglobin

NO sensing in Pseudomonas aeruginosa: structure of the transcriptional regulator DNR

Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator

The Structural Basis of Gas-Responsive Transcription by the Human Nuclear Hormone Receptor REV-ERBβ

Structural basis for cAMP-mediated allosteric control of the catabolite activator protein.

A dramatic conformational rearrangement is necessary for the activation of DNR from Pseudomonas aeruginosa. Crystal structure of wild-type DNR

Distal-to-proximal NO conversion in hemoproteins: the role of the proximal pocket

P2888

s10534-014-9770-3

P304

763-773

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P31

scholarly article

P356

10.1007/S10534-014-9770-3

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P433

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P478

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

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2014-07-10T00:00:00Z

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P5875

263816220

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P698

25007853

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P921

binding pocket

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

about

P2860

P2860

Distal-proximal crosstalk in the heme binding pocket of the NO sensor DNR.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921