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Literature summary extracted from

  • Shimizu, H.; Obayashi, E.; Gomi, Y.; Arakawa, H.; Park, S.Y.; Nakamura, H.; Adachi, S.I.; Shoun, H.; Shiro, Y.
    Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes (2000), J. Biol. Chem., 275, 4816-4826.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.2.5 at cryogenic temperature -173°C wild-type, S286V- and S286T-mutant Fusarium oxysporum

Protein Variants

EC Number Protein Variants Comment Organism
1.7.2.5 S286T 7% activity of wild-type Fusarium oxysporum
1.7.2.5 S286V 1% activity of wild-type Fusarium oxysporum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.5 Fe
-
Fusarium oxysporum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.5 2 nitric oxide + reduced acceptor Fusarium oxysporum
-
nitrous oxide + acceptor + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.5 Fusarium oxysporum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.5 2 nitric oxide + reduced acceptor
-
Fusarium oxysporum nitrous oxide + acceptor + H2O
-
?
1.7.2.5 2 nitric oxide + reduced acceptor NAD(P)H and NAD(P)+ as electron donor/acceptor Fusarium oxysporum nitrous oxide + acceptor + H2O
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.5 heme
-
Fusarium oxysporum
1.7.2.5 NADH
-
Fusarium oxysporum