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Literature summary for 1.7.2.1 extracted from

  • Basu, S.; Azarova, N.A.; Font, M.D.; King, S.B.; Hogg, N.; Gladwin, M.T.; Shiva, S.; Kim-Shapiro, D.B.
    Nitrite reductase activity of cytochrome c (2008), J. Biol. Chem., 283, 32590-32597.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Iron nitrite reductase activitiy of cytochrome c is dependent on the pentacoordination of the heme iron Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nitrite + electron donor Bos taurus mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration NO + oxidized electron donor + H2O
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Organism

Organism UniProt Comment Textmining
Bos taurus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Bos taurus
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heart
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Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + electron donor mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration Bos taurus NO + oxidized electron donor + H2O
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Cofactor

Cofactor Comment Organism Structure
heme nitrite reductase activitiy of cytochrome c is dependent on the pentacoordination of the heme iron Bos taurus