Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

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Expanding the substrates for a bacterial hydrogenlyase reaction.Keeping the spotlight on cytochrome P450.Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins.Improving artificial metalloenzymes' activity by optimizing electron transfer.

P2860

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P2860

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

Item

http://www.wikidata.org/entity/Q42414347

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

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2016年论文

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2016年论文

@zh-cn

name

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

@en

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

@nl

type

Item

label

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

@en

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

@nl

prefLabel

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

@en

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

@nl

P1476

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

@en

P2093

Silas Busck Mellor

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P2860

Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution

Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system

Transgenic tobacco and Arabidopsis plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in Dhurrin biosynthesis

Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer

Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum

The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity.

A post genomic characterization of Arabidopsis ferredoxins.

Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.

Cyanogenic glycosides: synthesis, physiology, and phenotypic plasticity.

Structure and function of plant-type ferredoxins.

P304

1862-1869

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P31

scholarly article

P356

10.1021/ACSCHEMBIO.6B00190

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P433

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

P478

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P50

Birger Lindberg Møller

Mohammed S Motawia

Dainius Jakubauskas

Agnieszka Zygadlo Nielsen

Meike Burow

Poul Erik Jensen

P577

2016-04-27T00:00:00Z

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P698

27119279

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P932

4949584

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Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

about

P2860

P2860

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

description

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932