Jump to content

Ferredoxin—nitrate reductase

From Wikipedia, the free encyclopedia
ferredoxin—nitrate reductase
Identifiers
EC no.1.7.7.2
CAS no.60382-69-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a ferredoxin—nitrate reductase (EC 1.7.7.2) is an enzyme that catalyzes the chemical reaction

nitrite + H2O + 2 oxidized ferredoxin nitrate + 2 reduced ferredoxin + 2 H+

The 3 substrates of this enzyme are nitrite, H2O, and oxidized ferredoxin, whereas its 3 products are nitrate, reduced ferredoxin, and H+. Nitrate Reductase is an essential enzyme present in most biological systems such as green plants, certain fungi, yeasts and bacteria that aids in the reduction of nitrate to ammonium.[1]

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 nitrite:ferredoxin oxidoreductase. Other names in common use include assimilatory nitrate reductase, nitrate (ferredoxin) reductase, and assimilatory ferredoxin-nitrate reductase. This enzyme participates in nitrogen metabolism. It has 4 cofactors: iron, Sulfur, Molybdenum, and Iron-sulfur. The Iron-Sulfur cluster ([4FE-4S]) in this enzyme has a variety of different functions that contribute to the growth of aerobic cells. Some of the functions include but are not limited to the following: involved in photosynthetic processes, electron-transfer reactions and the binding of certain substrates, resulting in activation.[2]

Structural studies

[edit]

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1PFD.

References

[edit]
  1. ^ Chamizo-Ampudia A, Sanz-Luque E, Llamas A, Galvan A, Fernandez E (February 2017). "Nitrate Reductase Regulates Plant Nitric Oxide Homeostasis". Trends in Plant Science. 22 (2): 163–174. doi:10.1016/j.tplants.2016.12.001. hdl:10396/29213. PMID 28065651.
  2. ^ Imsande J (February 1999). "Iron-sulfur clusters: Formation, perturbation, and physiological functions". Plant Physiology and Biochemistry. 37 (2): 87–97. doi:10.1016/S0981-9428(99)80070-9.

Further reading

[edit]
  • Mikami B, Ida S (December 1984). "Purification and properties of ferredoxin—nitrate reductase from the cyanobacterium Plectonema boryanum". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 791 (3): 294–304. doi:10.1016/0167-4838(84)90340-6.