Linked Life Data

37931

Source:http://linkedlifedata.com/resource/pubmed/id/37931

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1979-10-24
pubmed:abstractText
NAD+ reduction catalyzed by transhydrogenase (EC 1.6.1.1) from E. coli membrane particles at the expense of NADPH oxidation is coupled with phenyldicarbaundecaborate (PCB-) absorption by the particles. This process is inhibited by oxidative phosphorylation protonophorous uncouplers and by equilibration of concentrations of the substrates and products of the transhydrogenase reaction. Elimination of the water-soluble part of membrane ATPase results in the inhibition of PCB- absorption at the expense of the transhydrogenase reaction energy. Treatment of the particles by dicyclohexyl carbodiimide increases the transhydrogenase-coupled absorption of PCB-. The transhydrogenase-induced increase of pPCB in the suspension of particles is directly correlated with the ratio of ([NADPH].[NAD+])/([NADP+].[NADH]). When this value is equal to 1, no energy-dependent increase of pPCB was observed. NADP+ reduction at the expense of NADH oxidation leads to a decrease in the amount of PCB- absorbed by the particles at the expense of ATP hydrolysis energy. The experimental data suggest that NADPH oxidation in the course of the transhydrogenase reaction is coupled with the formation of a membrane potential with a positive charge localized inside the particles.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1101-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
[Transhydrogenase as an additional site of energy accumulation in the E. coli respiratory chain].
pubmed:publicationType
Journal Article, English Abstract