Impact of Proximal and Distal Pocket Site-Directed Mutations on the Ferric/Ferrous Heme Redox Potential of Yeast Cytochrome-c-Peroxidase

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Impact of Proximal and Distal Pocket Site-Directed Mutations on the Ferric/Ferrous Heme Redox Potential of Yeast Cytochrome-c-Peroxidase

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http://www.wikidata.org/entity/Q36681320

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2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Impact of Proximal and Distal ...... Yeast Cytochrome-c-Peroxidase

@ast

Impact of Proximal and Distal ...... Yeast Cytochrome-c-Peroxidase

@en

type

Item

label

Impact of Proximal and Distal ...... Yeast Cytochrome-c-Peroxidase

@ast

Impact of Proximal and Distal ...... Yeast Cytochrome-c-Peroxidase

@en

prefLabel

Impact of Proximal and Distal ...... Yeast Cytochrome-c-Peroxidase

@ast

Impact of Proximal and Distal ...... Yeast Cytochrome-c-Peroxidase

@en

P1476

Impact of Proximal and Distal ...... Yeast Cytochrome-c-Peroxidase

@en

P2093

D B Goodin

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

G M Jensen

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

P2860

Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase

Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure

Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein

High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase

X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis

Construction of a bisaquo heme enzyme and binding by exogenous ligands

Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase

The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme

Altering substrate specificity at the heme edge of cytochrome c peroxidase

A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity

P2888

s00214-011-1062-1

P304

1185-1196

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P31

scholarly article

P356

10.1007/S00214-011-1062-1

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

P433

4-6

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

P478

130

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

P577

2011-12-01T00:00:00Z

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

P5875

236057829

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

P698

23505335

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P932

3596509

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