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Synonyms
cytochrome c-552, cytochrome c nitrite reductase, ccnir, tvnir, nrfha, octahaem cytochrome c nitrite reductase, hexaheme c-type cytochrome, cytochrome c nitrite reductase complex, multiheme cytochrome c nitrite reductase, sco2488,
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hydroxylamine + reduced benzyl viologen
? + oxidized benzyl viologen
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nitrite + ferrocytochrome c + H+
NH3 + H2O + ferricytochrome c
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
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sulfite + 6 ferrocytochrome c + 6 H+
H2S + 3 H2O + 6 ferricytochrome c
nitrite + 6 ferrocytochrome c + 7 H+
NH3 + 2 H2O + 6 ferricytochrome c
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mechanism
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additional information
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nitrite + ferrocytochrome c + H+
NH3 + H2O + ferricytochrome c
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nitrite + ferrocytochrome c + H+
NH3 + H2O + ferricytochrome c
ccNiR catalyzes the six-electron reduction of nitrite to ammonia as the final step in the dissimilatory pathway of nitrate ammonification
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nitrite + ferrocytochrome c + H+
NH3 + H2O + ferricytochrome c
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
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sulfite + 6 ferrocytochrome c + 6 H+
H2S + 3 H2O + 6 ferricytochrome c
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sulfite + 6 ferrocytochrome c + 6 H+
H2S + 3 H2O + 6 ferricytochrome c
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
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additional information
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ccNiR also reduces sulfite to sulfide linking the biogeochemical cycles of nitrogen and of sulfur
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additional information
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ccNiR also reduces sulfite to sulfide linking the biogeochemical cycles of nitrogen and of sulfur
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additional information
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simulation of the kinetics of the reduction process reveals that the complex recharging process can be accomplished in two possible ways: either through two consecutive proton-coupled electron transfers or in the form of three consecutive elementary steps involving reduction, proton-coupled electron transfers and protonation. Recharging through two proton-coupled electron transfers is a means of overcoming the predicted deep energetic minimum that is calculated to occur at the stage of the Fe(II)-NO radical intermediate. The radical transfer role for the active-site Tyr218, cannot be confirmed. The highly conserved calcium located in the direct proximity of the active site plays an important role in the substrate conversion through the facilitation of the proton transfer steps
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additional information
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the first event in the second halfcycle is the reduction of the HNO intermediate, which is accomplished by two proton-coupled electron transfer reactions. Two isomeric radical intermediates, HNOH radial and H2NO radical, are formed. Both intermediates are readily transformed into hydroxylamine, most likely through intramolecular proton transfer from either Arg114 or His277. An extra proton must enter the active site of the enzyme to initiate heterolytic cleavage of the N-O bond. As a result of N-O bond cleavage, the H2N+ intermediate is formed. It picks up an electron, forming H2N+ radical, which in turn reacts with Tyr218. The intramolecular reaction with Tyr218 in the final step of the nitrite reduction process leads directly to the final product, ammonia. Dissociation of the final product proceeds concomitantly with a change in spin state
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additional information
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the enzyme catalyzes the last step in the metabolic pathway of nitrate dissimilation
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Liu, M.C.; Bakel, B.W.; Liu, M.Y.; Dao, T.N.
Purification of Vibrio fischeri nitrite reductase and its characterization as a hexaheme c-type cytochrome
Arch. Biochem. Biophys.
262
259-265
1988
Aliivibrio fischeri, Desulfovibrio desulfuricans, Escherichia coli K-12, Wolinella succinogenes
brenda
Einsle, O.; Stach, P.; Messerschmidt, A.; Simon, J.; Kroger, A.; Huber, R.; Kroneck, P.M.H.
Cytochrome c nitrite reductase from Wolinella succinogenes structure at 1.6.ANG. resolution, inhibitor binding, and heme-packing motifs
J. Biol. Chem.
275
39608-39616
2000
Wolinella succinogenes (Q9S1E5), Wolinella succinogenes
brenda
Einsle, O.; Stach, P.; Messerschmidt, A.; Klimmek, O.; Simon, J.; Kroger, A.; Kroneck, P.M.
Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes
Acta Crystallogr. Sect. D
58
341-342
2002
Wolinella succinogenes
brenda
Schumacher, W.; Hole, U.; Kroneck, P.M.
Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties
Biochem. Biophys. Res. Commun.
205
911-916
1994
Sulfurospirillum deleyianum, Wolinella succinogenes
brenda
Einsle, O.; Messerschmidt, A.; Huber, R.; Kroneck, P.M.; Neese, F.
Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase
J. Am. Chem. Soc.
124
11737-11745
2002
Wolinella succinogenes
brenda
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
Biochemistry
47
2080-2086
2008
Wolinella succinogenes (Q9S1E5), Wolinella succinogenes
brenda
Bykov, D.; Neese, F.
Substrate binding and activation in the active site of cytochrome c nitrite reductase: a density functional study
J. Biol. Inorg. Chem.
16
417-430
2011
Wolinella succinogenes (Q9S1E5)
brenda
Kern, M.; Volz, J.; Simon, J.
The oxidative and nitrosative stress defence network of Wolinella succinogenes: cytochrome c nitrite reductase mediates the stress response to nitrite, nitric oxide, hydroxylamine and hydrogen peroxide
Environ. Microbiol.
13
2478-2494
2011
Wolinella succinogenes (Q9S1E5), Wolinella succinogenes, Wolinella succinogenes ATCC 29543 (Q9S1E5)
brenda
Bykov, D.; Neese, F.
Reductive activation of the heme iron-nitrosyl intermediate in the reaction mechanism of cytochrome c nitrite reductase: a theoretical study
J. Biol. Inorg. Chem.
17
741-760
2012
Wolinella succinogenes (Q9S1E5), Wolinella succinogenes ATCC 29543 (Q9S1E5)
brenda
Lockwood, C.W.; Burlat, B.; Cheesman, M.R.; Kern, M.; Simon, J.; Clarke, T.A.; Richardson, D.J.; Butt, J.N.
Resolution of key roles for the distal pocket histidine in cytochrome C nitrite reductases
J. Am. Chem. Soc.
137
3059-3068
2015
Escherichia coli (P0ABK9), Wolinella succinogenes (Q9S1E5), Wolinella succinogenes DSM 1740 (Q9S1E5)
brenda
Bykov, D.; Plog, M.; Neese, F.
Heme-bound nitroxyl, hydroxylamine, and ammonia ligands as intermediates in the reaction cycle of cytochrome c nitrite reductase a theoretical study
J. Biol. Inorg. Chem.
19
97-112
2014
Wolinella succinogenes (Q9S1E5), Wolinella succinogenes DSM 1740 (Q9S1E5)
brenda