Kinetic characterization of the Escherichia coli nitric oxide reductase flavorubredoxin (Q37146613)

18 August 2017

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title

Kinetic characterization of the Escherichia coli nitric oxide reductase flavorubredoxin (English)

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Francesca Maria Scandurra

18 August 2017

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João B Vicente

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Elena Forte

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Alessandro Giuffrè

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Paolo Sarti

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Miguel Teixeira

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Maurizio Brunori

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series ordinal

object named as

Francesca M Scandurra

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18 August 2017

language of work or name

English

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publication date

1 January 2008

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18 August 2017

published in

Methods in Enzymology

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18 August 2017

volume

437

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18 August 2017

page(s)

47-62

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Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas

18 August 2017

cites work

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Regulation of the flavorubredoxin nitric oxide reductase gene inEscherichia coli: nitrate repression, nitrite induction, and possible post-transcription control

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Structure of a dioxygen reduction enzyme from Desulfovibrio gigas

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7 January 2021

Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli

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7 January 2021

A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin

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Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin

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7 January 2021

Spectroscopic studies and characterization of a novel electron-transfer chain from Escherichia coli involving a flavorubredoxin and its flavoprotein reductase partner

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New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide.

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Desulfovibrio gigas flavodiiron protein affords protection against nitrosative stress in vivo.

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The role of the flavodiiron proteins in microbial nitric oxide detoxification.

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F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification

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Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O

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A flavodiiron protein and high molecular weight rubredoxin from Moorella thermoacetica with nitric oxide reductase activity

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A flavo-diiron protein from Desulfovibrio vulgaris with oxidase and nitric oxide reductase activities. Evidence for an in vivo nitric oxide scavenging function.

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X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase

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Cytochrome c Oxidase Does Not Catalyze the Anaerobic Reduction of NO

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7 January 2021

Kinetics of electron transfer from NADH to the Escherichia coli nitric oxide reductase flavorubredoxin.

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Redox and spectroscopic properties of the Escherichia coli nitric oxide-detoxifying system involving flavorubredoxin and its NADH-oxidizing redox partner.

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A family of flavoproteins in the domains Archaea and Bacteria

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10.1016/S0076-6879(07)37003-1

Identifiers

DOI

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18 August 2017

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