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Literature summary for 1.15.1.2 extracted from

  • Clay, M.D.; Cosper, C.A.; Jenney, F.E.; Adams, M.W.; Johnson, M.K.
    Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase (2003), Proc. Natl. Acad. Sci. USA, 100, 3796-3801.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus P82385
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Reaction

Reaction Comment Organism Reaction ID
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin catalytic mechanism with the first step involving oxidative addition of superoxide to form a ferric-peroxo intermediate. The Fe spin state and the trans cysteinate ligand play an important role in effecting superoxide reduction and peroxide release Pyrococcus furiosus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information nitric oxide is used as a substrate analog to explore the structural and electronic determinants of enzymatic superoxide reduction at the mononuclear iron active site of Pyrococcus furiosus superoxide reductase through the use of EPR, resonance Raman, Fourier transform IR, UV-visible absorption, and variabletemperature variable-field magnetic CD spectroscopies Pyrococcus furiosus ?
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