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Literature summary for 1.7.2.5 extracted from

  • Vicente, J.B.; Scandurra, F.M.; Forte, E.; Brunori, M.; Sarti, P.; Teixeira, M.; Giuffre, A.
    Kinetic characterization of the Escherichia coli nitric oxide reductase flavorubredoxin (2008), Methods Enzymol., 437, 47-62.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NO + reduced acceptor Escherichia coli FlRd may protect Escherichia coli against NO, catalyzing the anaerobic reduction of NO to N2O N2O + H2O + acceptor
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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NO reductase activity is measured under anaerobic conditions using a NO-selective Clark-type electrode. Spectroscopic measurements using a stopped-flow thermostated instrument Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NO + reduced acceptor
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Escherichia coli N2O + H2O + acceptor
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NO + reduced acceptor FlRd may protect Escherichia coli against NO, catalyzing the anaerobic reduction of NO to N2O Escherichia coli N2O + H2O + acceptor
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Synonyms

Synonyms Comment Organism
FlRd
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Escherichia coli
nitric oxide reductase
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Escherichia coli