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Literature summary for 1.14.14.47 extracted from

  • Hannibal, L.; Somasundaram, R.; Tejero, J.; Wilson, A.; Stuehr, D.
    Influence of heme-thiolate in shaping the catalytic properties of a bacterial nitric-oxide synthase (2011), J. Biol. Chem., 286, 39224-39235.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
W66F mutation changes midpoint potential from -361 mV for wild-type to -427 mV. Mutant displays 2.5fold lower activity when reaction is supported by flavoproteins or NADPH instead of tetrahydrofolate Bacillus subtilis
W66H mutation changes midpoint potential from -361 mV for wild-type to -302 mV. Activity is similar to wild-type Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron in the presence of L-arginine and tetrahydrofolate, wild-type and mutants W66F and W66H exist in the typical Fe(III) high-spin configuration Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-arginine + 3 reduced flavodoxin + 4 O2
-
Bacillus subtilis 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
-
?

Cofactor

Cofactor Comment Organism Structure
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
Bacillus subtilis
additional information enzyme is able to use several different redox partners Bacillus subtilis
NADPH
-
Bacillus subtilis
tetrahydrofolate
-
Bacillus subtilis