Source:http://linkedlifedata.com/resource/pubmed/id/17541778
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2007-9-17
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pubmed:abstractText |
Metabolism of ammonia (NH(3)) and hydroxylamine (NH(2)OH) by wild-type and a nitrite reductase (nirK) deficient mutant of Nitrosomonas europaea was investigated to clarify the role of NirK in the NH(3) oxidation pathway. NirK-deficient N. europaea grew more slowly, consumed less NH(3), had a lower rate of nitrite (NO(2) (-)) production, and a significantly higher rate of nitrous oxide (N(2)O) production than the wild-type when incubated with NH(3) under high O(2) tension. In incubations with NH(3) under low O(2) tension, NirK-deficient N. europaea grew more slowly, but had only modest differences in NH(3) oxidation and product formation rates relative to the wild-type. In contrast, the nirK mutant oxidized NH(2)OH to NO(2) (-) at consistently slower rates than the wild-type, especially under low O(2) tension, and lost a significant pool of NH(2)OH-N to products other than NO(2) (-) and N(2)O. The rate of N(2)O production by the nirK mutant was ca. three times higher than the wild-type during hydrazine-dependent NO(2) (-) reduction under both high and low O(2) tension. Together, the results indicate that NirK activity supports growth of N. europaea by supporting the oxidation of NH(3) to NO(2) (-) via NH(2)OH, and stimulation of hydrazine-dependent NO(2) (-) reduction by NirK-deficient N. europaea indicated the presence of an alternative, enzymatic pathway for N(2)O production.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ammonia,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrazines,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxylamine,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrite Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrites,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrous Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/hydrazine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0302-8933
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
188
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
349-54
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pubmed:meshHeading |
pubmed-meshheading:17541778-Ammonia,
pubmed-meshheading:17541778-Bacterial Proteins,
pubmed-meshheading:17541778-Gene Deletion,
pubmed-meshheading:17541778-Hydrazines,
pubmed-meshheading:17541778-Hydroxylamine,
pubmed-meshheading:17541778-Nitrite Reductases,
pubmed-meshheading:17541778-Nitrites,
pubmed-meshheading:17541778-Nitrosomonas europaea,
pubmed-meshheading:17541778-Nitrous Oxide,
pubmed-meshheading:17541778-Oxidation-Reduction,
pubmed-meshheading:17541778-Oxygen
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pubmed:year |
2007
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pubmed:articleTitle |
Role of nitrite reductase in the ammonia-oxidizing pathway of Nitrosomonas europaea.
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pubmed:affiliation |
Department of Environmental Sciences, Geology 2207, University of California, Riverside, CA 92521, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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