From Wikipedia, the free encyclopedia
Hydroxylamine dehydrogenase
Identifiers
EC no. 1.7.2.6
CAS no. 9075-43-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
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PMC articles
PubMed articles
NCBI proteins

Hydroxylamine dehydrogenase ( EC 1.7.2.6, HAO (ambiguous)) is an enzyme with systematic name hydroxylamine:ferricytochrome-c oxidoreductase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

(1) hydroxylamine + H2O + 2 ferricytochrome c nitrite + 2 ferrocytochrome c + 5 H+
(2) hydroxylamine + ferricytochrome c nitric oxide + ferrocytochrome c + 3 H+

The enzymes from the nitrifying bacterium Nitrosomonas europaea and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins.

References

  1. ^ Rees MK (January 1968). "Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I. Purification of hydroxylamine oxidase". Biochemistry. 7 (1): 353–66. doi: 10.1021/bi00841a045. PMID  5758552.
  2. ^ Hooper AB, Terry KR (November 1979). "Hydroxylamine oxidoreductase of Nitrosomonas. Production of nitric oxide from hydroxylamine". Biochimica et Biophysica Acta. 571 (1): 12–20. doi: 10.1016/0005-2744(79)90220-1. PMID  497235.
  3. ^ Hooper AB, Balny C (August 1982). "Reaction of oxygen with hydroxylamine oxidoreductase of Nitrosomonas: fast kinetics". FEBS Letters. 144 (2): 299–303. doi: 10.1016/0014-5793(82)80658-3. PMID  7117545. S2CID  9726167.
  4. ^ Lipscomb JD, Hooper AB (August 1982). "Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy". Biochemistry. 21 (17): 3965–72. doi: 10.1021/bi00260a010. PMID  6289867.
  5. ^ Poret-Peterson AT, Graham JE, Gulledge J, Klotz MG (December 2008). "Transcription of nitrification genes by the methane-oxidizing bacterium, Methylococcus capsulatus strain Bath". The ISME Journal. 2 (12): 1213–20. doi: 10.1038/ismej.2008.71. PMID  18650926.

External links

From Wikipedia, the free encyclopedia
Hydroxylamine dehydrogenase
Identifiers
EC no. 1.7.2.6
CAS no. 9075-43-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Hydroxylamine dehydrogenase ( EC 1.7.2.6, HAO (ambiguous)) is an enzyme with systematic name hydroxylamine:ferricytochrome-c oxidoreductase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

(1) hydroxylamine + H2O + 2 ferricytochrome c nitrite + 2 ferrocytochrome c + 5 H+
(2) hydroxylamine + ferricytochrome c nitric oxide + ferrocytochrome c + 3 H+

The enzymes from the nitrifying bacterium Nitrosomonas europaea and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins.

References

  1. ^ Rees MK (January 1968). "Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I. Purification of hydroxylamine oxidase". Biochemistry. 7 (1): 353–66. doi: 10.1021/bi00841a045. PMID  5758552.
  2. ^ Hooper AB, Terry KR (November 1979). "Hydroxylamine oxidoreductase of Nitrosomonas. Production of nitric oxide from hydroxylamine". Biochimica et Biophysica Acta. 571 (1): 12–20. doi: 10.1016/0005-2744(79)90220-1. PMID  497235.
  3. ^ Hooper AB, Balny C (August 1982). "Reaction of oxygen with hydroxylamine oxidoreductase of Nitrosomonas: fast kinetics". FEBS Letters. 144 (2): 299–303. doi: 10.1016/0014-5793(82)80658-3. PMID  7117545. S2CID  9726167.
  4. ^ Lipscomb JD, Hooper AB (August 1982). "Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy". Biochemistry. 21 (17): 3965–72. doi: 10.1021/bi00260a010. PMID  6289867.
  5. ^ Poret-Peterson AT, Graham JE, Gulledge J, Klotz MG (December 2008). "Transcription of nitrification genes by the methane-oxidizing bacterium, Methylococcus capsulatus strain Bath". The ISME Journal. 2 (12): 1213–20. doi: 10.1038/ismej.2008.71. PMID  18650926.

External links


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