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	<title>Quadratic set - Revision history</title>
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	<updated>2026-05-23T13:18:40Z</updated>
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		<title>en&gt;Ag2gaeh: /* References */</title>
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		<updated>2014-01-21T15:43:02Z</updated>

		<summary type="html">&lt;p&gt;&lt;span class=&quot;autocomment&quot;&gt;References&lt;/span&gt;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;{{Infobox enzyme&lt;br /&gt;
| Name = Hydroxylamine dehydrogenase&lt;br /&gt;
| EC_number = 1.7.2.6&lt;br /&gt;
| CAS_number = 9075-43-8&lt;br /&gt;
| IUBMB_EC_number = 1/7/2/6&lt;br /&gt;
| GO_code = &lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption =&lt;br /&gt;
}}&lt;br /&gt;
&amp;#039;&amp;#039;&amp;#039;Hydroxylamine dehydrogenase&amp;#039;&amp;#039;&amp;#039; ({{EC number|1.7.2.6}}, &amp;#039;&amp;#039;HAO (ambiguous)&amp;#039;&amp;#039;) is an [[enzyme]] with system name &amp;#039;&amp;#039;hydroxylamine:ferricytochrome-c oxidoreductase&amp;#039;&amp;#039;.&amp;lt;ref&amp;gt;{{cite journal | title = Studies of the hydroxylamine metabolism of &amp;lt;em&amp;gt;Nitrosomonas europaea&amp;lt;/em&amp;gt;. I. Purification of hydroxylamine oxidase |author = Rees, M. |journal = Biochemistry |year = 1968 |volume = 7 |pages = 353–366 |pmid = 5758552 |doi=10.1021/bi00841a045}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Hydroxylamine oxidoreductase of &amp;lt;em&amp;gt;Nitrosomonas&amp;lt;/em&amp;gt;. Production of nitric oxide from hydroxylamine |author = Hooper, A.B. and Terry, K.R. |journal = Biochim. Biophys. Acta |year = 1979 |volume = 571 |pages = 12–20 |pmid = 497235 |issue=1}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Reaction of oxygen with hydroxylamine oxidoreductase of &amp;lt;em&amp;gt;Nitrosomonas&amp;lt;/em&amp;gt;: fast kinetics |author = Hooper, A.B. and Balny, C. |journal = FEBS Lett. |year = 1982 |volume = 144 |pages = 299–303 |pmid = 7117545 |doi=10.1016/0014-5793(82)80658-3}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Resolution of multiple heme centers of hydroxylamine oxidoreductase from &amp;lt;em&amp;gt;Nitrosomonas&amp;lt;/em&amp;gt;. 1. Electron paramagnetic resonance spectroscopy |author = Lipscomb, J.D. and Hooper, A.B. |journal = Biochemistry |year = 1982 |volume = 21 |pages = 3965–3972 |pmid = 6289867 |doi=10.1021/bi00260a010}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Transcription of nitrification genes by the methane-oxidizing bacterium, &amp;lt;em&amp;gt;Methylococcus capsulatus&amp;lt;/em&amp;gt; strain Bath |author = Poret-Peterson, A.T., Graham, J.E., Gulledge, J. and Klotz, M.G. |journal = ISME J. |year = 2008 |volume = 2 |pages = 1213–1220 |pmid = 18650926 |doi=10.1038/ismej.2008.71 |issue=12}}&amp;lt;/ref&amp;gt; This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
: (1) [[hydroxylamine]] + H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O + 2 ferricytochrome c &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; nitrite + 2 ferrocytochrome c + 5 H&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt;&lt;br /&gt;
: (2) [[hydroxylamine]] + ferricytochrome c &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; [[nitric oxide]] + ferrocytochrome c + 3 H&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt;&lt;br /&gt;
&lt;br /&gt;
The enzymes from the [[Nitrifying bacteria|nitrifying bacterium]] &amp;#039;&amp;#039;[[Nitrosomonas europaea]]&amp;#039;&amp;#039; and the methylotrophic bacterium &amp;#039;&amp;#039;[[Methylococcus capsulatus]]&amp;#039;&amp;#039; are [[hemoprotein]]s.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
{{reflist}}&lt;br /&gt;
&lt;br /&gt;
== External links ==&lt;br /&gt;
* {{MeshName|Hydroxylamine+dehydrogenase}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 1.7.2]]&lt;/div&gt;</summary>
		<author><name>en&gt;Ag2gaeh</name></author>
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