Distal pocket control of nitrite binding in myoglobin - Wikidata - awgldk - TriplyDB

Distal pocket control of nitrite binding in myoglobin

Distal pocket control of nitrite binding in myoglobin

http://www.wikidata.org/entity/Q27677563

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Nitrite binding to globins: linkage isomerism, EPR silence and reductive chemistry.Outer-sphere oxidation of Fe(II) in nitrosylmyoglobin by ferricyanide Functional tuning and expanding of myoglobin by rational protein design

P2860

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P2860

Distal pocket control of nitrite binding in myoglobin

http://www.wikidata.org/entity/Q27677563

description

2012 nî lūn-bûn

@nan

2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

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

name

Distal pocket control of nitrite binding in myoglobin

@ast

Distal pocket control of nitrite binding in myoglobin

@en

Distal pocket control of nitrite binding in myoglobin

@nl

type

label

Distal pocket control of nitrite binding in myoglobin

@ast

Distal pocket control of nitrite binding in myoglobin

@en

Distal pocket control of nitrite binding in myoglobin

@nl

prefLabel

Distal pocket control of nitrite binding in myoglobin

@ast

Distal pocket control of nitrite binding in myoglobin

@en

Distal pocket control of nitrite binding in myoglobin

@nl

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P1433

Angewandte Chemie International Edition

P1476

Distal pocket control of nitrite binding in myoglobin

@en

P2093

George B Richter-Addo

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

Jun Yi

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

Leonard M Thomas

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

P2860

Binding and reduction of sulfite by cytochrome c nitrite reductase

The nitrite anion binds to human hemoglobin via the uncommon O-nitrito mode

High-resolution structural analysis of a novel octaheme cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens

The Distal Pocket Histidine Residue in Horse Heart Myoglobin Directs the O -Binding Mode of Nitrite to the Heme Iron

Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase

Formation of the complex of nitrite with the ferriheme b beta-barrel proteins nitrophorin 4 and nitrophorin 7

Synchrotron X-ray-induced photoreduction of ferric myoglobin nitrite crystals gives the ferrous derivative with retention of the O-bonded nitrite ligand.

Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme

Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products

Metalloenzymes of the denitrification pathway

P304

3625-7

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scholarly article

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10.1002/ANIE.201200010

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P407

P433

15

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P478

51

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2012-04-10T00:00:00Z

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P698

22383424

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