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Literature summary for 1.7.1.3 extracted from

  • Kalimuthu, P.; Kruse, T.; Bernhardt, P.
    Deconstructing the electron transfer chain in a complex molybdoenzyme Assimilatory nitrate reductase from Neurospora crassa (2021), Biochim. Biophys. Acta Bioenerg., 1862, 148358 .
    View publication on PubMed
Search for more literature for 1.7.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Neurospora crassa

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum a functional nitrate reductase can be generated that lacks both the FAD and heme cofactors leaving the Mo active site as the sole redox active centre Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrate + NADPH + H+
-
 Neurospora crassa nitrite + NADP+ + H2O
-
 ?
nitrate + reduced anthraquinone 2-sulfonate
-
 Neurospora crassa nitrite + anthraquinone 2-sulfonate
-
 ?
nitrate + reduced benzyl viologen
-
 Neurospora crassa nitrite + benzyl viologen
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Neurospora crassa
heme
-
 Neurospora crassa

General Information

General Information Comment Organism
metabolism catalytic voltammetry of enzyme variants on a modified Au electrode with the electrochemically reduced forms of benzyl viologen and anthraquinone sulfonate as artificial electron donors. The biopolymer chitosan entraps nitrate reductase on the electrode noncovalently. Both an enzyme form lacking the FAD cofactor and one lacking both the FAD and heme cofactors show catalytic nitrate reductase activity, removal of the heme cofactor results in a more significant effect on the rate of nitrate reduction Neurospora crassa