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Literature summary for 1.7.2.2 extracted from

  • Ali, M.; Stein, N.; Mao, Y.; Shahid, S.; Schmidt, M.; Bennett, B.; Pacheco, A.A.
    Trapping of a putative intermediate in the cytochrome c nitrite Reductase (ccNiR)-catalyzed reduction of nitrite Implications for the ccNiR reaction mechanism (2019), J. Am. Chem. Soc., 141, 13358-13371 .
    View publication on PubMed
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Application

Application Comment Organism
analysis trapping of a putative intermediate by controlling the electrochemical potential at which reduction takes place. An [FeNO}]7 active site is a catalytic intermediate in the ccNiR-mediated reduction of nitrite to ammonia. At low potentials the species is rapidly reduced and does not accumulate, while at higher potentials it is trapped, thus preventing catalytic ammonia formation Shewanella oneidensis

Organism

Organism UniProt Comment Textmining
Shewanella oneidensis Q8EAC7
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Synonyms

Synonyms Comment Organism
ccNiR
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 Shewanella oneidensis
cytochrome c nitrite reductase
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 Shewanella oneidensis
cytochrome c-552
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 Shewanella oneidensis
NrfA
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 Shewanella oneidensis

General Information

General Information Comment Organism
metabolism nitrite-loaded ccNiR is reduced in a concerted two-electron step to generate an [FeNO]7 moiety at the active site, with an associated midpoint potential of +246 mV vs standard hydrogen electrode at pH 7. Cyanide-bound active site reduction is a one-electron process with a midpoint potential of +20 mV, and without a strong-field ligand the active site midpoint potential shifts 70 mV lower still. The [FeNO]7 moiety possesses an spectral signature, different from those normally observed for [FeNO]7 hemes, that may indicate magnetic interaction of the active site with nearby hemes. Catalytic nitrite reduction to ammonia by ccNiR requires an applied potential of at least -120 mV, well below the midpoint potential for [FeNO]7 formation Shewanella oneidensis