Rahul Sharma (Editor)

Cytochrome c nitrite reductase

Updated on
Edit
Like
Comment
Share on FacebookTweet on TwitterShare on LinkedInShare on Reddit
EC number
  
1.7.2.2

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

MetaCyc
  
metabolic pathway

Cytochrome c nitrite reductase

Cytochrome c nitrite reductase (ccNiR) (EC 1.7.2.2) is a bacterial enzyme that catalyzes the six electron reduction of nitrite to ammonia; an important step in the biological nitrogen cycle. The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during anaerobic conditions. During this process, ccNiR draws electrons from the quinol pool, which are ultimately provided by a dehydrogenase such as formate dehydrogenase or hydrogenase. These dehydrogenases are responsible for generating a proton motive force.

Cytochrome c Nitrite Reductase is a homodimer which contains five c-type heme cofactors per monomer. Four of the heme centers are bis-histidine ligated and presumably serve to shuttle electrons to the active site. The active site heme, however, is uniquely ligated by a single lysine residue.

This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is ammonia:ferricytochrome-c oxidoreductase.

References

Cytochrome c nitrite reductase Wikipedia