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Literature summary for 1.7.2.2 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
Search for more literature for 1.7.2.2

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Wolinella succinogenes ccNiR also reduces sulfite to sulfide linking the biogeochemical cycles of nitrogen and of sulfur ?
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 ?
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
-
 ?
sulfite + 6 ferrocytochrome c + 6 H+ Wolinella succinogenes
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 H2S + 3 H2O + 6 ferricytochrome c
-
 ?

Organism

Organism UniProt Comment Textmining
Wolinella succinogenes Q9S1E5
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ccNiR also reduces sulfite to sulfide linking the biogeochemical cycles of nitrogen and of sulfur Wolinella succinogenes ?
-
 ?
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
-
 ?
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
-
 ?
sulfite + 6 ferrocytochrome c + 6 H+
-
 Wolinella succinogenes H2S + 3 H2O + 6 ferricytochrome c
-
 ?
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
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 ?

Subunits

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

Synonyms

Synonyms Comment Organism
ccNiR
-
 Wolinella succinogenes
cytochrome c nitrite reductase
-
 Wolinella succinogenes

Cofactor

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