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・ Cytochalasin E
・ Cytochemistry
・ Cytochrome
・ Cytochrome b
・ Cytochrome b-245
・ Cytochrome b-245, alpha polypeptide
・ Cytochrome b5
・ Cytochrome b5 reductase
・ Cytochrome b5, type A
・ Cytochrome b559
・ Cytochrome b561
・ Cytochrome b6f complex
・ Cytochrome c
・ Cytochrome c assembly protein family
・ Cytochrome c family
Cytochrome c nitrite reductase
・ Cytochrome c oxidase
・ Cytochrome c oxidase subunit I
・ Cytochrome c oxidase subunit II
・ Cytochrome c oxidase subunit III
・ Cytochrome c oxidase subunit Vb
・ Cytochrome c peroxidase
・ Cytochrome c reductase
・ Cytochrome C1
・ Cytochrome d
・ Cytochrome f
・ Cytochrome P450
・ Cytochrome P450 reductase
・ Cytochrome P450, family 1, member A1
・ Cytochrome-c3 hydrogenase


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Cytochrome c nitrite reductase : ウィキペディア英語版
Cytochrome c nitrite reductase

Cytochrome ''c'' nitrite reductase (ccNiR) () 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==


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