Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450. - sprookjes - yvandenbroek - TriplyDB

Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

http://www.wikidata.org/entity/Q30378241

about

Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.Genetic Optimization of Metalloenzymes: Enhancing Enzymes for Non-Natural Reactions.Exploiting and engineering hemoproteins for abiological carbene and nitrene transfer reactions.Identification of Mechanism-Based Inactivation in P450-Catalyzed Cyclopropanation Facilitates Engineering of Improved Enzymes.Mutating a Highly Conserved Residue in Diverse Cytochrome P450s Facilitates Diastereoselective Olefin Cyclopropanation.An artificial metalloenzyme with the kinetics of native enzymes.Preface

P2860

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P2860

Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

http://www.wikidata.org/entity/Q30378241

description

2015 nî lūn-bûn

@nan

2015 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի օգոստոսին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

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Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

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type

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Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

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Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

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Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

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Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

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Journal of the American Chemical Society

P1476

Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

@en

P2093

Andrew R Buller

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

John A McIntosh

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

Linda Chio

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Thomas Heel

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P2860

Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus

Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties

A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo

Construction of a bisaquo heme enzyme and binding by exogenous ligands

Olefin Cyclopropanation via Carbene Transfer Catalyzed by Engineered Cytochrome P450 Enzymes

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

Structural analysis of heme proteins: implications for design and prediction.

Involvement of a cytochrome P450 monooxygenase in thaxtomin A biosynthesis by Streptomyces acidiscabies.

Enzyme-controlled nitrogen-atom transfer enables regiodivergent C-H amination.

P450 BM3: the very model of a modern flavocytochrome.

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13861-13865

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scholarly article

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10.1021/JACS.5B07107

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43

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137

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2015-08-24T00:00:00Z

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281262018

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26299431

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4635421

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