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Literature summary extracted from

  • Lukat, P.; Rudolf, M.; Stach, P.; Messerschmidt, A.; Kroneck, P.M.; Simon, J.; Einsle, O.
    Binding and reduction of sulfite by cytochrome c nitrite reductase (2008), Biochemistry, 47, 2080-2086.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.2.2 ccNIR as apoenzyme or with bound sulfite or nitrite to the catalytic heme center, X-ray diffraction structure determination and analysis at 1.30-1.75 A resolution Wolinella succinogenes

Protein Variants

EC Number Protein Variants Comment Organism
1.7.2.2 Y218F active site mutant, that shows almost complete loss of nitrite reductase activity, while sulfite reduction remains unaffected Wolinella succinogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.2 Iron pentaheme cytochrome c nitrite reductase Wolinella succinogenes

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.2 additional information Wolinella succinogenes ccNiR also reduces sulfite to sulfide linking the biogeochemical cycles of nitrogen and of sulfur ?
-
 ?
1.7.2.2 nitrite + ferrocytochrome c + H+ Wolinella succinogenes ccNiR catalyzes the six-electron reduction of nitrite to ammonia as the final step in the dissimilatory pathway of nitrate ammonification NH3 + H2O + ferricytochrome c
-
 ?
1.7.2.2 sulfite + 6 ferrocytochrome c + 6 H+ Wolinella succinogenes
-
 H2S + 3 H2O + 6 ferricytochrome c
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.2 Wolinella succinogenes Q9S1E5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.2 additional information ccNiR also reduces sulfite to sulfide linking the biogeochemical cycles of nitrogen and of sulfur Wolinella succinogenes ?
-
 ?
1.7.2.2 nitrite + ferrocytochrome c + H+ ccNiR catalyzes the six-electron reduction of nitrite to ammonia as the final step in the dissimilatory pathway of nitrate ammonification Wolinella succinogenes NH3 + H2O + ferricytochrome c
-
 ?
1.7.2.2 nitrite + ferrocytochrome c + H+ nitrite is the preferred substrate. ccNiR is encoded by gene nrfA performing nitrite reduction with formate. Sulfite and nitrite both provide a pair of electrons to form the coordinative bond to the Fe(III) active site of the enzyme Wolinella succinogenes NH3 + H2O + ferricytochrome c
-
 ?
1.7.2.2 sulfite + 6 ferrocytochrome c + 6 H+
-
 Wolinella succinogenes H2S + 3 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 sulfite + 6 ferrocytochrome c + 6 H+ sulfite and nitrite both provide a pair of electrons to form the coordinative bond to the Fe(III) active site of the enzyme, and the oxygen atoms of sulfite are found to interact with the three active site protein residues conserved within the enzyme family, binding mode of sulfite to the catalytic heme center of ccNiR, overview Wolinella succinogenes H2S + 3 H2O + 6 ferricytochrome c
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.2 oligomer ccNiR 's threedimensional structure shows the characteristically close packing of heme cofactors into parallel and perpendicular motifs Wolinella succinogenes

Synonyms

EC Number Synonyms Comment Organism
1.7.2.2 ccNiR
-
 Wolinella succinogenes
1.7.2.2 cytochrome c nitrite reductase
-
 Wolinella succinogenes

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.2 heme pentaheme cytochrome c nitrite reductase Wolinella succinogenes