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Literature summary for 1.7.2.1 extracted from

  • Prudencio, M.; Eady, R.R.; Sawers, G.
    Catalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: implications for substrate interaction (2001), Biochem. J., 353, 259-266.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.7.2.1

Cloned(Commentary)

Cloned (Comment) Organism
D92E and D92N mutant enzyme Achromobacter xylosoxidans

Protein Variants

Protein Variants Comment Organism
D92E mutation in type 2 Cu center, very low activity with artificial electron donors methyl viologen and sodium dithionite, 20-30% of wild-type activity with physiological electron donor azurin I Achromobacter xylosoxidans
D92N mutation in type 2 Cu center, very low activity with artificial electron donors methyl viologen and sodium dithionite, 60-70% of wild-type activity with physiological electron donor azurin I Achromobacter xylosoxidans
H139A mutation in type 1 Cu center, very low activity with the artificial electron donor methyl viologen, no activity with the physiological electron donor azurin I Achromobacter xylosoxidans

Metals/Ions

Metals/Ions Comment Organism Structure
copper the type 1 Cu center functions as electron acceptor from the physiological electron donor azurin I, the type 2 Cu center is involved in binding and reduction of the substrate Achromobacter xylosoxidans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced azurin + O2 Achromobacter xylosoxidans putative physiological electron donor oxidized azurin + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Achromobacter xylosoxidans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and D92E and D92N mutant enzyme Achromobacter xylosoxidans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
45.2
-
 native recombinant enzyme, azurin Achromobacter xylosoxidans
107
-
 native recombinant enzyme, dithionite Achromobacter xylosoxidans
168
-
 native recombinant enzyme, methyl viologen Achromobacter xylosoxidans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + ferrocytochrome c
-
 Achromobacter xylosoxidans nitric oxide + H2O + ferricytochrome c
-
 ?
NO2- + reduced azurin putative physiological electron donor Achromobacter xylosoxidans NO + oxidized azurin
-
 ?
reduced azurin + O2 putative physiological electron donor Achromobacter xylosoxidans oxidized azurin + H2O
-
 ?