(Q39774882)

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Oxygen-insensitive nitroreductases NfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent Azo reductases

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scholarly article

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Europe PubMed Central

PMC publication ID

14 September 2017

Oxygen-insensitive nitroreductases NfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent Azo reductases (English)

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Escherichia coli

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author name string

Jörg Rau

1

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Andreas Stolz

2

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Europe PubMed Central

PMC publication ID

14 September 2017

language of work or name

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publication date

1 June 2003

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Europe PubMed Central

PMC publication ID

14 September 2017

Applied and Environmental Microbiology

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Europe PubMed Central

PMC publication ID

14 September 2017

69

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Europe PubMed Central

PMC publication ID

14 September 2017

6

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

3448-3455

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F.

1 reference

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Phytodetoxification of TNT by transgenic plants expressing a bacterial nitroreductase.

1 reference

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22 September 2017

Basic and applied aspects in the microbial degradation of azo dyes

1 reference

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Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution

1 reference

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Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme

1 reference

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22 September 2017

The function of cytoplasmic flavin reductases in the reduction of azo dyes by bacteria

1 reference

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22 September 2017

Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli.

1 reference

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Humic acids as electron acceptors for anaerobic microbial oxidation of vinyl chloride and dichloroethene.

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1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins

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Reduction of azo dyes by redox mediators originating in the naphthalenesulfonic acid degradation pathway of Sphingomonas sp. strain BN6.

1 reference

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Conversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution

1 reference

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22 September 2017

Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase

1 reference

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22 September 2017

Crystal Structure ofEscherichia coliQOR Quinone Oxidoreductase Complexed with NADPH

1 reference

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22 September 2017

A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments

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22 September 2017

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

1 reference

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22 September 2017

The metabolism of azo compounds: a review of the literature

1 reference

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22 September 2017

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain.

1 reference

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22 September 2017

Azoreductase activity of anaerobic bacteria isolated from human intestinal microflora

1 reference

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22 September 2017

Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae

1 reference

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22 September 2017

The reduction of azo dyes by the intestinal microflora

1 reference

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Oxygen-sensitive and -insensitive nitroreduction by Escherichia coli and rat hepatic microsomes

1 reference

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25 September 2017

Localization of the Enzyme System Involved in Anaerobic Reduction of Azo Dyes by Sphingomonas sp. Strain BN6 and Effect of Artificial Redox Mediators on the Rate of Azo Dye Reduction

1 reference

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Effects of different quinoid redox mediators on the anaerobic reduction of azo dyes by bacteria

1 reference

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Type I nitroreductases in soil enterobacteria reduce TNT (2,4,6,-trinitrotoluene) and RDX (hexahydro-1,3,5-trinitro-1,3,5-triazine).

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Purification and characterization of wild-type and mutant "classical" nitroreductases of Salmonella typhimurium. L33R mutation greatly diminishes binding of FMN to the nitroreductase of S. typhimurium.

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Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri

1 reference

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Characterization of FMN-dependent NADH-quinone reductase induced by menadione in Escherichia coli.

1 reference

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Cloning, nucleotide sequence, and expression of the nitroreductase gene from Enterobacter cloacae.

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An investigation of dye reduction by food-borne bacteria

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The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)--I. Purification and properties of a nitroreductase enzyme from Escherichia coli--a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT).

1 reference

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Exogenous quinones directly inhibit the respiratory NADH dehydrogenase in Escherichia coli

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Reduction of Azo Food Dyes in Cultures ofProteus vulgaris

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Type I nitroreductases of Escherichia coli.

1 reference

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Steady-state kinetic mechanism, stereospecificity, substrate and inhibitor specificity of Enterobacter cloacae nitroreductase

1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/12788749

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1 reference

https://pubmed.ncbi.nlm.nih.gov/12788749

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Redox Potentials and Quinone Reductase Activity ofl-Aspartate Oxidase fromEscherichia coli†

1 reference

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Identifiers

10.1128/AEM.69.6.3448-3455.2003

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

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