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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1997-11-25
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pubmed:abstractText |
Nitrite reductase from Pseudomonas aeruginosa (NiR-Pa) is a dimer consisting of two identical 60 kDa subunits, each of which contains one c and one d1 heme group. This enzyme, a soluble component of the electron-transfer chain that uses nitrate as a source of energy, can be induced by the addition of nitrate to the bacterial growth medium. NiR-Pa catalyzes the reduction of nitrite (NO2-) to nitric oxide (NO); in vitro, both cytochrome c551 and azurin are efficient electron donors in this reaction. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1157-71
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9331415-Amino Acid Sequence,
pubmed-meshheading:9331415-Bacterial Proteins,
pubmed-meshheading:9331415-Binding Sites,
pubmed-meshheading:9331415-Catalysis,
pubmed-meshheading:9331415-Crystallization,
pubmed-meshheading:9331415-Crystallography, X-Ray,
pubmed-meshheading:9331415-Cytochrome c Group,
pubmed-meshheading:9331415-Dimerization,
pubmed-meshheading:9331415-Heme,
pubmed-meshheading:9331415-Hemeproteins,
pubmed-meshheading:9331415-Hydrogen Bonding,
pubmed-meshheading:9331415-Models, Molecular,
pubmed-meshheading:9331415-Molecular Sequence Data,
pubmed-meshheading:9331415-Nitrite Reductases,
pubmed-meshheading:9331415-Nitrites,
pubmed-meshheading:9331415-Protein Conformation,
pubmed-meshheading:9331415-Protein Structure, Secondary,
pubmed-meshheading:9331415-Pseudomonas aeruginosa,
pubmed-meshheading:9331415-Sequence Alignment,
pubmed-meshheading:9331415-Water
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pubmed:year |
1997
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pubmed:articleTitle |
N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa.
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pubmed:affiliation |
Architecture et Fonction des Macromolécules Biologiques, U.P.R. 9039-C.N.R.S., I.B.S.M., Marseille, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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