Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

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Activation and inactivation of horseradish peroxidase by cobalt ions.

P2860

Q46556608-334AB150-D591-4DF3-B357-05E5D9C12695

P2860

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

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http://www.wikidata.org/entity/Q43979202

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2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

2002年學術文章

@zh-hant

name

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

@en

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

@nl

type

Item

label

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

@en

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

@nl

prefLabel

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

@en

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

@nl

P1476

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

@en

P2093

Hai-Meng Zhou

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

Hong-Wei Zhou

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

Yan Xu

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

P2860

Crystal structure of horseradish peroxidase C at 2.15 A resolution

Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography

Chimeric molecules employing horseradish peroxidase as reporter enzyme for protein localization in the electron microscope.

Apohorseradish peroxidase unfolding and refolding: intrinsic tryptophan fluorescence studies.

Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome c

pH-induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide-modified enzymes.

Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis.

Improvement of peroxygenase activity by relocation of a catalytic histidine within the active site of horseradish peroxidase.

Haem propionates control oxidative and reductive activities of horseradish peroxidase by maintaining the correct orientation of the haem.

The steady-state kinetics of peroxidase with 2,2'-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen.

P304

205-213

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

P31

scholarly article

P356

10.1139/O02-003

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

P433

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

P478

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

P577

2002-01-01T00:00:00Z

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

P698

11989716

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

P921

Horseradish peroxidase

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

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P2860

P2860

Activity and conformational changes of horseradish peroxidase in trifluoroethanol.

description

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type

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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