Matches in SemOpenAlex for { <https://semopenalex.org/work/W2042022104> ?p ?o ?g. }
Showing items 1 to 74 of
74
with 100 items per page.
- W2042022104 abstract "Low potential quinones are mediators of cyclic phosphorylation in washed spinach thylakoid membranes if they are prereduced to provide the proper redox poise. Cyclic phosphorylation catalyzed by different quinols varies in its sensitivity to the electron transfer inhibitor 2-iodo-6-isopropyl-3-methyl-2',4,4'-trinitrodiphenyl ether (DNPINT), which is thought to inhibit electron flux from the bound plastoquinone (B) to the plastoquinone pool (Trebst, A., Wietoska, H., Draber, W. and Knops, H.J. (1978) Z. Naturforsch. 33c, 919-927). Cyclic phosphorylation catalyzed by uncharged quinols is extremely sensitive to DNPINT, whereas cyclic phosphorylation catalyzed by negatively charged quinols is approximately two orders of magnitude less sensitive. Many quinols have pK1 values in the physiological range (pH 7-9). Increasing the concentration of the deprotonated quinol either by raising the assay pH, increasing the mediator concentration, or increasing the fractional reduction of the quinone results in a decrease in the sensitivity of cyclic phosphorylation to DNPINT. At very high DNPINT concentrations, cyclic phosphorylation catalyzed by all quinols (and ferredoxin) is inhibited, but not phenazine methosulfate catalyzed cyclic phosphorylation. These data suggest that the deprotonated form of the quinol can donate electrons directly to the plastoquinone pool, whereas the uncharged quinol most obligately transfer electrons through the bound plastoquinone 'B'. A second site of DNPINT action after the plastoquinone pool is also observed, which requires much higher DNPINT concentrations for inhibition of phosphorylation." @default.
- W2042022104 created "2016-06-24" @default.
- W2042022104 creator A5017860234 @default.
- W2042022104 creator A5032189773 @default.
- W2042022104 date "1980-09-01" @default.
- W2042022104 modified "2023-09-27" @default.
- W2042022104 title "Two pathways of electron transfer in quinol-mediated cyclic phosphorylation in spinach chloroplasts" @default.
- W2042022104 cites W1973784366 @default.
- W2042022104 cites W1974907033 @default.
- W2042022104 cites W1979377289 @default.
- W2042022104 cites W2001656846 @default.
- W2042022104 cites W2003784665 @default.
- W2042022104 cites W2003939826 @default.
- W2042022104 cites W2005157079 @default.
- W2042022104 cites W2011182262 @default.
- W2042022104 cites W2020272429 @default.
- W2042022104 cites W2029107743 @default.
- W2042022104 cites W2034768894 @default.
- W2042022104 cites W2037440092 @default.
- W2042022104 cites W2070155274 @default.
- W2042022104 cites W2080626590 @default.
- W2042022104 cites W2089505625 @default.
- W2042022104 cites W2162132666 @default.
- W2042022104 doi "https://doi.org/10.1016/0005-2728(80)90192-9" @default.
- W2042022104 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7407095" @default.
- W2042022104 hasPublicationYear "1980" @default.
- W2042022104 type Work @default.
- W2042022104 sameAs 2042022104 @default.
- W2042022104 citedByCount "11" @default.
- W2042022104 crossrefType "journal-article" @default.
- W2042022104 hasAuthorship W2042022104A5017860234 @default.
- W2042022104 hasAuthorship W2042022104A5032189773 @default.
- W2042022104 hasConcept C101692577 @default.
- W2042022104 hasConcept C104317684 @default.
- W2042022104 hasConcept C11960822 @default.
- W2042022104 hasConcept C123669783 @default.
- W2042022104 hasConcept C12554922 @default.
- W2042022104 hasConcept C185592680 @default.
- W2042022104 hasConcept C24840226 @default.
- W2042022104 hasConcept C2779515454 @default.
- W2042022104 hasConcept C55493867 @default.
- W2042022104 hasConcept C69305403 @default.
- W2042022104 hasConcept C75473681 @default.
- W2042022104 hasConcept C86803240 @default.
- W2042022104 hasConceptScore W2042022104C101692577 @default.
- W2042022104 hasConceptScore W2042022104C104317684 @default.
- W2042022104 hasConceptScore W2042022104C11960822 @default.
- W2042022104 hasConceptScore W2042022104C123669783 @default.
- W2042022104 hasConceptScore W2042022104C12554922 @default.
- W2042022104 hasConceptScore W2042022104C185592680 @default.
- W2042022104 hasConceptScore W2042022104C24840226 @default.
- W2042022104 hasConceptScore W2042022104C2779515454 @default.
- W2042022104 hasConceptScore W2042022104C55493867 @default.
- W2042022104 hasConceptScore W2042022104C69305403 @default.
- W2042022104 hasConceptScore W2042022104C75473681 @default.
- W2042022104 hasConceptScore W2042022104C86803240 @default.
- W2042022104 hasLocation W20420221041 @default.
- W2042022104 hasLocation W20420221042 @default.
- W2042022104 hasOpenAccess W2042022104 @default.
- W2042022104 hasPrimaryLocation W20420221041 @default.
- W2042022104 hasRelatedWork W1963751191 @default.
- W2042022104 hasRelatedWork W1997816279 @default.
- W2042022104 hasRelatedWork W2009868513 @default.
- W2042022104 hasRelatedWork W2012380986 @default.
- W2042022104 hasRelatedWork W2071799724 @default.
- W2042022104 hasRelatedWork W2072041321 @default.
- W2042022104 hasRelatedWork W2082348233 @default.
- W2042022104 hasRelatedWork W2084305467 @default.
- W2042022104 hasRelatedWork W2740692208 @default.
- W2042022104 hasRelatedWork W2796361136 @default.
- W2042022104 isParatext "false" @default.
- W2042022104 isRetracted "false" @default.
- W2042022104 magId "2042022104" @default.
- W2042022104 workType "article" @default.