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Literature summary for 1.7.2.4 extracted from

  • DellAcqua, S.; Pauleta, S.; Moura, J.; Moura, I.
    Biochemical characterization of the purple form of Marinobacter hydrocarbonoclasticus nitrous oxide reductase (2012), Philos. Trans. R. Soc. Lond. B Biol. Sci., 367, 1204-1212.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.7.2.4

Organism

Organism UniProt Comment Textmining
Marinobacter nauticus
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-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information the purple form of enzyme, in which the copper centre is in the oxidized [2Cu2+:2Cu+] redox state, is redox active, although it is still catalytically non-competent, as its specific activity is lower than that of the activated fully reduced enzyme and comparable with that of the enzyme with the copper centre in either the [1Cu2+:3Cu+] redox state or in the redox inactive state Marinobacter nauticus

Purification (Commentary)

Purification (Comment) Organism
isolation of the enzyme in the purple form, in which the copper centre is in the oxidized [2Cu2+:2Cu+] redox state and is redox active. Isolation of this form in the presence of oxygen from a microaerobic culture in the presence of nitrate and also from a strictly anaerobic culture Marinobacter nauticus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.4
-
 fully oxidized enzyme isolated from aerobic growth conditions, pH 7.6, temperature not specified in the publication Marinobacter nauticus
1.1
-
 fully oxidized enzyme isolated from aanerobic growth conditions, pH 7.6, temperature not specified in the publication Marinobacter nauticus
88
-
 fully reduced enzyme isolated from aerobic growth conditions, pH 7.6, temperature not specified in the publication Marinobacter nauticus
92.4
-
 fully reduced enzyme isolated from aerobic growth conditions, pH 7.6, temperature not specified in the publication Marinobacter nauticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the purple form of enzyme, in which the copper centre is in the oxidized [2Cu2+:2Cu+] redox state, is redox active, although it is still catalytically non-competent, as its specific activity is lower than that of the activated fully reduced enzyme and comparable with that of the enzyme with the copper centre in either the [1Cu2+:3Cu+] redox state or in the redox inactive state Marinobacter nauticus ?
-
 ?
N2O + reduced methyl viologen
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 Marinobacter nauticus N2 + H2O + oxidized methyl viologen
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 ?

Synonyms

Synonyms Comment Organism
N2OR
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 Marinobacter nauticus