Ferredoxin—nitrite reductase

In enzymology, a ferredoxin—nitrite reductase (EC 1.7.7.1) is an enzyme that catalyzes the chemical reaction

NH₃ + 2 H₂O + 6 oxidized ferredoxin ${\displaystyle \rightleftharpoons }$ nitrite + 6 reduced ferredoxin + 7 H⁺

The 3 substrates of this enzyme are NH₃, H₂O, and oxidized ferredoxin, whereas its 3 products are nitrite, reduced ferredoxin, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is ammonia:ferredoxin oxidoreductase. This enzyme participates in nitrogen metabolism and nitrogen assimilation. It has 3 cofactors: iron, Siroheme, and Iron-sulfur.

This enzyme can use many different isoforms of ferredoxin. In photosynthesizing tissues, it uses ferredoxin that is reduced by PSI and in the root it uses a form of ferredoxin (FdIII) that has a less negative midpoint potential and can be reduced easily by NADPH.^[1]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1ZJ8, 1ZJ9, and 2AKJ.

References

Literature