Linked Life Data

8919448

Source:http://linkedlifedata.com/resource/pubmed/id/8919448

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-5-12
pubmed:abstractText
Anaerobic metabolism of the simplest, best understood enteric bacteria such as Escherichia coli is unexpectedly complex. Recent studies of the biochemistry and genetics of nitrate reduction via nitrite to ammonia by enteric bacteria have provided insights into the reasons for this complexity. An NADH-dependent nitrite reductase in the cytoplasm works in partnership with the respiratory nitrate reductase on the cytoplasmic side of the membrane when nitrate is abundant. There is also an electrogenic, formate-dependent nitrite reductase ready to work in partnership with a periplasmic nitrate reductase when nitrite is available but nitrate is scarce. A third E. coli nitrate reductase, NarZYWV, and the poorly expressed formate dehydrogenase O possibly facilitate rapid adaptation to oxygen starvation pending the synthesis of the major respiratory formate-nitrate oxidoreductase. Although most anaerobically expressed genes are subject to transcription control, none of them are totally switched off. This enables the bacteria to be ready for a change in fortune: when growing anaerobically with nitrate, they can respond equally rapidly whether times get better with the arrival of oxygen, or get worse when the nitrate is depleted. Far from being redundant, the complexity is essential for survival in a changing environment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
136
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-11
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation?
pubmed:affiliation
School of Biochemistry, University of Birmingham, UK.
pubmed:publicationType
Journal Article, Review