Calculated and experimental spin state of seleno cytochrome P450. - Wikidata - wikimedia - TriplyDB

Calculated and experimental spin state of seleno cytochrome P450.

Calculated and experimental spin state of seleno cytochrome P450.

http://www.wikidata.org/entity/Q33766095

about

Engineering P450 Peroxygenase to Catalyze Highly Enantioselective Epoxidation of cis-β-Methylstyrenes.A novel intermediate in the reaction of seleno CYP119 with m-chloroperbenzoic acid Analysis of cytochrome P450 CYP119 ligand-dependent conformational dynamics by two-dimensional NMR and X-ray crystallography.Proximal ligand electron donation and reactivity of the cytochrome P450 ferric-peroxo anion Cytochrome P450-type hydroxylation and epoxidation in a tyrosine-liganded hemoprotein, catalase-related allene oxide synthase.Spectroscopic studies of the cytochrome P450 reaction mechanisms.Characterization of a selenocysteine-ligated P450 compound I reveals direct link between electron donation and reactivity.Selenium and Selenocysteine in Protein Chemistry.Potential drug targets in the Mycobacterium tuberculosis cytochrome P450 system.

P2860

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P2860

Calculated and experimental spin state of seleno cytochrome P450.

http://www.wikidata.org/entity/Q33766095

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

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name

Calculated and experimental spin state of seleno cytochrome P450.

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Calculated and experimental spin state of seleno cytochrome P450.

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type

label

Calculated and experimental spin state of seleno cytochrome P450.

@ast

Calculated and experimental spin state of seleno cytochrome P450.

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prefLabel

Calculated and experimental spin state of seleno cytochrome P450.

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Calculated and experimental spin state of seleno cytochrome P450.

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P1433

Angewandte Chemie International Edition

P1476

Calculated and experimental spin state of seleno cytochrome P450

@en

P2093

Paul R Ortiz de Montellano

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Santhosh Sivaramakrishnan

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Sason Shaik

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

Shimrit Cohen

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Yongying Jiang

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P2860

Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine

Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam.

In silico design of a mutant of cytochrome P450 containing selenocysteine.

Selenolate complexes of CYP101 and the heme-bound hHO-1/H25A proximal cavity mutant

Roles of the proximal heme thiolate ligand in cytochrome p450(cam).

The active site of the thermophilic CYP119 from Sulfolobus solfataricus.

Cytochrome P450cam and its complexes. Mössbauer parameters of the heme iron.

Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues.

Characterization of the oxygenated intermediate of the thermophilic cytochrome P450 CYP119.

Replacement of active-site cysteine-436 by serine converts cytochrome P450 2B4 into an NADPH oxidase with negligible monooxygenase activity.

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7193-7195

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scholarly article

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10.1002/ANIE.200901485

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39

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48

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Takahiro Hayashi

Pierre Moenne-Loccoz

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2009-01-01T00:00:00Z

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26778486

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19718734

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2848667

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