Linked Life Data

2269422

Source:http://linkedlifedata.com/resource/pubmed/id/2269422

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1991-2-19
pubmed:abstractText
Three sites of inhibitory action of hydroxylamine were identified in the respiratory chain of anaerobically grown bacterium Paracoccus denitrificans. Terminal oxidases were blocked at concentrations of 10(-4) to 10(-3) mol.l-1, and the inhibitor competed with artificial donor of electrons N, N, N', N'-tetramethyl-l, 4-phenylenediamine. In the anaerobic part of the respiratory chain inhibition of nitrite reductase and apparently also nitric oxide reductase occurred, resulting in the increased accumulation of nitric oxide during denitrification. These effects together with the inhibition of terminal oxidases by nitric oxide are probably realized through switching the electron flow from oxygen to nitrogen terminal acceptors in the presence of hydroxylamine. By means of difference spectroscopy, the respiratory inhibitor mucidin and a cytochrome c-deficient mutant of Paracoccus denitrificans, hydroxylamine could be shown to serve also as a terminal acceptor of the cytochrome c region. Reduction of hydroxylamine to ammonia was at the same time accompanied by the formation of transmembrane electrical gradient. Hydroxylamine reductase was purified 123-fold from the periplasmatic cell fraction by FPLC; the product obtained showed the features of respiratory nitrite reductase of the cytochrome cd1 type.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0231-5882
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
501-17
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Hydroxylamine as an inhibitor and terminal acceptor in the respiratory chain of the bacterium Paracoccus denitrificans.
pubmed:affiliation
Department of Biochemistry, Faculty of Science, Masaryk University, Brno, Czechoslovakia.
pubmed:publicationType
Journal Article