Linked Life Data

8920986

Source:http://linkedlifedata.com/resource/pubmed/id/8920986

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1996-12-30
pubmed:abstractText
The characterization of the hydroxylamine oxidase from the heterotrophic nitrifier Paracoccus denitrificans GB17 indicates the enzyme to be entirely distinct from the hydroxylamine oxidase from the autotrophic nitrifier Nitrosomonas europaea. Hydroxylamine oxidase from P. denitrificans contains three to five non-haem, non-iron-sulphur iron atoms as prosthetic groups, predominantly co-ordinated by carboxylate ligands. The interaction of the enzyme with the electron-accepting proteins cytochrome C556 and pseudoazurin is mainly hydrophobic. The catalytic mechanism of hydroxylamine oxidase from P. denitrificans is different from the enzyme from N. europaea because the production of nitrite by the former requires molecular oxygen. Under anaerobic conditions the enzyme makes nitrous oxide as a sole product.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
319 ( Pt 3)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
823-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17.
pubmed:affiliation
School of Biological Sciences, University of East Anglia, Norwich, U.K.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't