Hydroxylamine dehydrogenase

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Hydroxylamine dehydrogenase
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EC no. 1.7.2.6
CAS no. 9075-43-8
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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.

Related Research Articles

<i>Nitrosomonas</i> Genus of bacteria

Nitrosomonas is a genus of Gram-negative bacteria, belonging to the Betaproteobacteria. It is one of the five genera of ammonia-oxidizing bacteria and, as an obligate chemolithoautotroph, uses ammonia as an energy source and carbon dioxide as a carbon source in presence of oxygen. Nitrosomonas are important in the global biogeochemical nitrogen cycle, since they increase the bioavailability of nitrogen to plants and in the denitrification, which is important for the release of nitrous oxide, a powerful greenhouse gas. This microbe is photophobic, and usually generate a biofilm matrix, or form clumps with other microbes, to avoid light. Nitrosomonas can be divided into six lineages: the first one includes the species Nitrosomonas europea, Nitrosomonas eutropha, Nitrosomonas halophila, and Nitrosomonas mobilis. The second lineage presents the species Nitrosomonas communis, N. sp. I and N. sp. II, meanwhile the third lineage includes only Nitrosomonas nitrosa. The fourth lineage includes the species Nitrosomonas ureae and Nitrosomonas oligotropha and the fifth and sixth lineages include the species Nitrosomonas marina, N. sp. III, Nitrosomonas estuarii and Nitrosomonas cryotolerans.

Trimethylamine N-oxide reductase is a microbial enzyme that can reduce trimethylamine N-oxide (TMAO) into trimethylamine (TMA), as part of the electron transport chain. The enzyme has been purified from E. coli and the photosynthetic bacteria Roseobacter denitrificans.

<span class="mw-page-title-main">Sulfite dehydrogenase</span>

In enzymology, a sulfite dehydrogenase (EC 1.8.2.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a Δ7-sterol 5(6)-desaturase is an enzyme that catalyzes the chemical reaction

In enzymology, a D-lactate dehydrogenase (cytochrome) is an enzyme that catalyzes the chemical reaction

In enzymology, a mannitol dehydrogenase (cytochrome) (EC 1.1.2.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a carbon-monoxide dehydrogenase (cytochrome b-561) (EC 1.2.2.4) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Formate dehydrogenase (cytochrome)</span> Type of enzyme

In enzymology, a formate dehydrogenase (cytochrome) (EC 1.2.2.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a formate dehydrogenase (cytochrome-c-553) (EC 1.2.2.3) is an enzyme that catalyzes the chemical reaction

Hydroxylamine oxidoreductase (HAO) is an enzyme found in the prokaryotic genus Nitrosomonas. It plays a critically important role in the biogeochemical nitrogen cycle as part of the metabolism of ammonia-oxidizing bacteria.

<span class="mw-page-title-main">Nitrite reductase (NO-forming)</span> Class of enzymes

In enzymology, a nitrite reductase (NO-forming) (EC 1.7.2.1) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Thiosulfate dehydrogenase</span>

Thiosulfate dehydrogenase is an enzyme that catalyzes the chemical reaction:

In enzymology, a trimethylamine-N-oxide reductase (cytochrome c) (EC 1.7.2.3) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Flavocytochrome c sulfide dehydrogenase</span>

Flavocytochrome c sulfide dehydrogenase, also known as Sulfide-cytochrome-c reductase (flavocytochrome c) (EC 1.8.2.3), is an enzyme with systematic name hydrogen-sulfide:flavocytochrome c oxidoreductase. It is found in sulfur-oxidising bacteria such as the purple phototrophic bacteria Allochromatium vinosum. This enzyme catalyses the following chemical reaction:

<span class="mw-page-title-main">Methanol dehydrogenase (cytochrome c)</span>

Methanol dehydrogenase (cytochrome c) (EC 1.1.2.7, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction

L-galactonolactone dehydrogenase (EC 1.3.2.3, galactonolactone dehydrogenase, L-galactono-gamma-lactone dehydrogenase, L-galactono-gamma-lactone:ferricytochrome-c oxidoreductase, GLDHase, GLDase) is an enzyme with systematic name L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction

Nitric oxide reductase (cytochrome c) (EC 1.7.2.5) is an enzyme with systematic name nitrous oxide:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction

Dimethyl sulfide:cytochrome c2 reductase (EC 1.8.2.4) is an enzyme with systematic name dimethyl sulfide:cytochrome-c2 oxidoreductase. It is also known by the name dimethylsulfide dehydrogenase (Ddh). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Methane monooxygenase (particulate)</span>

Methane monooxygenase (particulate) (EC 1.14.18.3) is an enzyme with systematic name methane,quinol:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction

Ammonia monooxygenase (EC 1.14.99.39, AMO) is an enzyme, which catalyses the following chemical reaction

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.
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