Matches in SemOpenAlex for { <https://semopenalex.org/work/W762816612> ?p ?o ?g. }
Showing items 1 to 78 of
78
with 100 items per page.
- W762816612 endingPage "69" @default.
- W762816612 startingPage "459" @default.
- W762816612 abstract "Isolated chloroplast ATP synthase (CF0F1) was used for determination of the structure-function relation by measuring the effect of divalent metal ions on the properties of ATPase. Mg2+ ions were more efficient catalysts than Ca2+ ions as indicated by Kcat/Km of 55.2 and 5.4, respectively. Other activity parameters related to binding, such as the Km of MATP and Ki of MADP, indicated a stronger binding in the presence of Mg2+ as seen from a Mg2+/Ca2+ ratio of 2.8 and 3.8, respectively. Strong binding of Ca2+ ions with a Kd of 0.03 +/- 00.6 microM-1 was detected only in the presence of ADP probably because of the positive interactive effect of CaADP as indicated in the inhibition properties. Mg2+ ions were more efficient catalysts also in other forms of the enzyme such as in the thylakoid membrane, in isolated CF0F1 and in CF1. The Mg2+/Ca2+ ratio of Kcat/Km was 5.3, 10.2 and 1.5 for the thylakoid membrane enzyme, the isolated CF0F1 and the soluble CF1 respectively. This indicated that Ca2+ ions became less efficient catalysts in the more intact and integrated enzyme while Mg2+ ions were as efficient in all forms of the enzyme. Unlike Mg2+, Ca2+ ions also did not support proton-coupled ATP synthesis and ATP driven proton pumping. It is suggested that the differences in the ligand structure of these two ions might be the reason for the differential function. An average 0.3 A shorter bond length of octahedral first coordination in Ca2+ ions caused a weaker binding of CaATP than that of MgATP. The effect of differential binding is discussed in relation to the binding of the transition state intermediate and to the rate of product release." @default.
- W762816612 created "2016-06-24" @default.
- W762816612 creator A5018557168 @default.
- W762816612 creator A5068000024 @default.
- W762816612 creator A5075390637 @default.
- W762816612 creator A5091724338 @default.
- W762816612 date "2000-12-01" @default.
- W762816612 modified "2023-09-23" @default.
- W762816612 title "Role of metal ions in coupling between chemical catalysis and conformational changes in ATP synthase." @default.
- W762816612 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11355634" @default.
- W762816612 hasPublicationYear "2000" @default.
- W762816612 type Work @default.
- W762816612 sameAs 762816612 @default.
- W762816612 citedByCount "1" @default.
- W762816612 crossrefType "journal-article" @default.
- W762816612 hasAuthorship W762816612A5018557168 @default.
- W762816612 hasAuthorship W762816612A5068000024 @default.
- W762816612 hasAuthorship W762816612A5075390637 @default.
- W762816612 hasAuthorship W762816612A5091724338 @default.
- W762816612 hasConcept C101692577 @default.
- W762816612 hasConcept C104317684 @default.
- W762816612 hasConcept C112243037 @default.
- W762816612 hasConcept C145148216 @default.
- W762816612 hasConcept C161790260 @default.
- W762816612 hasConcept C178790620 @default.
- W762816612 hasConcept C179104552 @default.
- W762816612 hasConcept C181199279 @default.
- W762816612 hasConcept C185592680 @default.
- W762816612 hasConcept C199164860 @default.
- W762816612 hasConcept C23265538 @default.
- W762816612 hasConcept C41183919 @default.
- W762816612 hasConcept C544153396 @default.
- W762816612 hasConcept C55493867 @default.
- W762816612 hasConcept C56856141 @default.
- W762816612 hasConcept C69305403 @default.
- W762816612 hasConcept C71240020 @default.
- W762816612 hasConcept C74884574 @default.
- W762816612 hasConcept C8010536 @default.
- W762816612 hasConceptScore W762816612C101692577 @default.
- W762816612 hasConceptScore W762816612C104317684 @default.
- W762816612 hasConceptScore W762816612C112243037 @default.
- W762816612 hasConceptScore W762816612C145148216 @default.
- W762816612 hasConceptScore W762816612C161790260 @default.
- W762816612 hasConceptScore W762816612C178790620 @default.
- W762816612 hasConceptScore W762816612C179104552 @default.
- W762816612 hasConceptScore W762816612C181199279 @default.
- W762816612 hasConceptScore W762816612C185592680 @default.
- W762816612 hasConceptScore W762816612C199164860 @default.
- W762816612 hasConceptScore W762816612C23265538 @default.
- W762816612 hasConceptScore W762816612C41183919 @default.
- W762816612 hasConceptScore W762816612C544153396 @default.
- W762816612 hasConceptScore W762816612C55493867 @default.
- W762816612 hasConceptScore W762816612C56856141 @default.
- W762816612 hasConceptScore W762816612C69305403 @default.
- W762816612 hasConceptScore W762816612C71240020 @default.
- W762816612 hasConceptScore W762816612C74884574 @default.
- W762816612 hasConceptScore W762816612C8010536 @default.
- W762816612 hasIssue "6" @default.
- W762816612 hasLocation W7628166121 @default.
- W762816612 hasOpenAccess W762816612 @default.
- W762816612 hasPrimaryLocation W7628166121 @default.
- W762816612 hasRelatedWork W177687039 @default.
- W762816612 hasRelatedWork W1972465018 @default.
- W762816612 hasRelatedWork W1976131890 @default.
- W762816612 hasRelatedWork W1994671970 @default.
- W762816612 hasRelatedWork W2002414094 @default.
- W762816612 hasRelatedWork W2025428586 @default.
- W762816612 hasRelatedWork W2071299881 @default.
- W762816612 hasRelatedWork W2084265096 @default.
- W762816612 hasRelatedWork W2952322977 @default.
- W762816612 hasRelatedWork W762816612 @default.
- W762816612 hasVolume "37" @default.
- W762816612 isParatext "false" @default.
- W762816612 isRetracted "false" @default.
- W762816612 magId "762816612" @default.
- W762816612 workType "article" @default.