Relationships of ligand binding, redox properties, and protonation in Coprinus cinereus peroxidase.

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How active-site protonation state influences the reactivity and ligation of the heme in chlorite dismutase.

P2860

Q34632613-BD11A731-4CB6-4CBE-A6BB-BCBCD4B3F01E

P2860

Relationships of ligand binding, redox properties, and protonation in Coprinus cinereus peroxidase.

Item

http://www.wikidata.org/entity/Q44350656

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Relationships of ligand bindin ...... Coprinus cinereus peroxidase.

@en

Relationships of ligand bindin ...... Coprinus cinereus peroxidase.

@nl

type

Item

label

Relationships of ligand bindin ...... Coprinus cinereus peroxidase.

@en

Relationships of ligand bindin ...... Coprinus cinereus peroxidase.

@nl

prefLabel

Relationships of ligand bindin ...... Coprinus cinereus peroxidase.

@en

Relationships of ligand bindin ...... Coprinus cinereus peroxidase.

@nl

P1476

Relationships of ligand bindin ...... Coprinus cinereus peroxidase.

@en

P2093

Antonella Rosati

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

Chiara Ciaccio

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

Federica Sinibaldi

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

Giampiero De Sanctis

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

Karen G Welinder

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

Massimo Coletta

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

Paolo Ascenzi

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

Roberto Santucci

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

Stefano Marini

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

P2860

Binding of iodide to Arthromyces ramosus peroxidase investigated with X-ray crystallographic analysis, 1H and 127I NMR spectroscopy, and steady-state kinetics

Crystal structure of horseradish peroxidase C at 2.15 A resolution

The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.

Flavohemoglobin, a globin with a peroxidase-like catalytic site.

How do enzymes work? Effect of electron circuits on transition state acid dissociation constants.

Versatility of heme coordination demonstrated in a fungal peroxidase. Absorption and resonance Raman studies of Coprinus cinereus peroxidase and the Asp245-->Asn mutant at various pH values.

The Asp245-->Asn mutant of Coprinus cinereus peroxidase. Characterization by 1H-NMR spectroscopy and comparison with the wild-type enzyme.

Mechanisms of cooperativity and allosteric regulation in proteins.

Hydrogen bonding modulates binding of exogenous ligands in a myoglobin proximal cavity mutant.

Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium: functional role of residues on the proximal side of the haem pocket.

P304

18730-18737

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P31

scholarly article

P356

10.1074/JBC.M212034200

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P407

English

P433

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

P478

278

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P577

2003-03-05T00:00:00Z

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

P698

12621034

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

P921

ligand binding

Relationships of ligand binding, redox properties, and protonation in Coprinus cinereus peroxidase.

about

P2860

P2860

Relationships of ligand binding, redox properties, and protonation in Coprinus cinereus peroxidase.

description

name

type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921