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Literature summary for 1.7.2.1 extracted from

  • Wijma, H.J.; Jeuken, L.J.; Verbeet, M.P.; Armstrong, F.A.; Canters, G.W.
    A random-sequential mechanism for nitrite binding and active site reduction in copper-containing nitrite reductase (2006), J. Biol. Chem., 281, 16340-16346.
    View publication on PubMed
Search for more literature for 1.7.2.1

Protein Variants

Protein Variants Comment Organism
M150T mutant enzyme has a type-1 site with a 125-mV higher midpoint potential and a 0.3-eV higher reorganization energy leading to an about 50-fold slower intramolecular electrontransfer to the type-2 site Alcaligenes faecalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Alcaligenes faecalis

Organism

Organism UniProt Comment Textmining
Alcaligenes faecalis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + reduced benzyl viologen random sequential mechanism Alcaligenes faecalis NO + oxidized benzyl viologen
-
 ?
nitrite + reduced methyl viologen random sequential mechanism Alcaligenes faecalis NO + oxidized methyl viologen
-
 ?
nitrite + reduced pseudoazurin random sequential mechanism Alcaligenes faecalis NO + oxidized pseudoazurin
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6
-
 reaction with 0.5 mM nitrite and pseudoazurin as electron donor Alcaligenes faecalis
6
-
 reaction with 5 mM nitrite and pseudoazurin as electron donor Alcaligenes faecalis

pH Range

pH Minimum pH Maximum Comment Organism
4.9 6.2 pH 4.9: about 55% of maximal ativity, pH 6.2: about 65% of maximal activity, reaction with 0.5 mM nitrite and pseudoazurin as electron donor Alcaligenes faecalis
5.2 6.5 pH 5.2: about 60% of maximal activity, pH 6.5: about 55% of maximal activity, reaction with 5 mM nitrite and pseudoazurin as electron donor Alcaligenes faecalis