FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2037504705> ?p ?o ?g. }

• W2037504705 endingPage "12211" @default.
• W2037504705 startingPage "12201" @default.
• W2037504705 abstract "The mutation E204Q in the β subunit of the chloroplast F1-ATPase was made by biolistic transformation of Chlamydomonas reinhardtii. The yield of chloroplast F1-ATPase (CF1) purified from thylakoids was unaltered, suggesting that the mutation did not affect protein assembly. However, photoautotrophic growth of Chlamydomonas strains containing βE204Q was virtually abolished, and the effect of the mutation on the light-driven ATPsynthase activity catalyzed by purified thylakoids was comparable to the change in the photoautotrophic growth rate. The loss of ATPsynthase activity in the mutant was not the result of uncoupling. Addition of wild-type CF1 to mutant thylakoids depleted of CF1 reconstituted ATPsynthase activity indicating that the mutation did not affect assembly of F0. Furthermore, the mutant CF1F0 was capable of catalyzing ATPase-dependent proton pumping as measured by fluorescence quenching of 9-amino acridine. Although the mutation significantly affected the apparent kcat/KM of the Mg2+-ATPase activity of the purified CF1-ATPase, no significant effect on the apparent kcat was observed with the mutant compared to wild-type. No significant changes in the ability of Mg2+ or Mn2+ to serve either as a cofactor or as an inhibitor of ATPase activity were observed in the mutants relative to the wild-type CF1-ATPase. EPR spectra were also taken of VO2+ bound at catalytic site 3 in its latent form. In a large fraction of the latent enzyme, a carboxyl group has displaced the nucleotide−phosphate coordination to the metal which results in the free-metal inhibited form (M3). No significant effects on the g∥ and A∥ 51V hyperfine parameters were observed between wild-type and mutant. However, the mutation increased the abundance of the M3 form relative to the M3−N3 form (metal−nucleotide-coordinated form). On the basis of these results, βE204 is not the carboxyl group that displaces the nucleotide phosphate as a ligand to form the free-metal inhibited enzyme form which predominates in site 3 in the latent state. Instead, the data are consistent with a role in which βE204 is essential to protonate an inorganic phosphate−oxygen to make that oxygen a good leaving group to facilitate ATP synthesis and, via this role in H-bonding, increases the abundance of the functional metal−nucleotide complex bound to the catalytic site." @default.
• W2037504705 created "2016-06-24" @default.
• W2037504705 creator A5042405907 @default.
• W2037504705 creator A5060943395 @default.
• W2037504705 creator A5065486802 @default.
• W2037504705 creator A5067676662 @default.
• W2037504705 creator A5069454696 @default.
• W2037504705 date "1996-01-01" @default.
• W2037504705 modified "2023-09-23" @default.
• W2037504705 title "Catalytic and EPR Studies of the βE204Q Mutant of the Chloroplast F₁-ATPase from <i>Chlamydomonas reinhardtii</i>" @default.
• W2037504705 cites W1482607235 @default.
• W2037504705 cites W1528014643 @default.
• W2037504705 cites W1560343559 @default.
• W2037504705 cites W1592367145 @default.
• W2037504705 cites W1593758392 @default.
• W2037504705 cites W1607491058 @default.
• W2037504705 cites W1991292465 @default.
• W2037504705 cites W2016712099 @default.
• W2037504705 cites W2045653785 @default.
• W2037504705 cites W2087256582 @default.
• W2037504705 cites W2164978892 @default.
• W2037504705 doi "https://doi.org/10.1021/bi961105a" @default.
• W2037504705 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8810928" @default.
• W2037504705 hasPublicationYear "1996" @default.
• W2037504705 type Work @default.
• W2037504705 sameAs 2037504705 @default.
• W2037504705 citedByCount "16" @default.
• W2037504705 countsByYear W20375047052022 @default.
• W2037504705 crossrefType "journal-article" @default.
• W2037504705 hasAuthorship W2037504705A5042405907 @default.
• W2037504705 hasAuthorship W2037504705A5060943395 @default.
• W2037504705 hasAuthorship W2037504705A5065486802 @default.
• W2037504705 hasAuthorship W2037504705A5067676662 @default.
• W2037504705 hasAuthorship W2037504705A5069454696 @default.
• W2037504705 hasConcept C101692577 @default.
• W2037504705 hasConcept C104317684 @default.
• W2037504705 hasConcept C143065580 @default.
• W2037504705 hasConcept C181199279 @default.
• W2037504705 hasConcept C185592680 @default.
• W2037504705 hasConcept C207583985 @default.
• W2037504705 hasConcept C23265538 @default.
• W2037504705 hasConcept C2776580309 @default.
• W2037504705 hasConcept C2777727519 @default.
• W2037504705 hasConcept C55493867 @default.
• W2037504705 hasConcept C69305403 @default.
• W2037504705 hasConcept C86803240 @default.
• W2037504705 hasConceptScore W2037504705C101692577 @default.
• W2037504705 hasConceptScore W2037504705C104317684 @default.
• W2037504705 hasConceptScore W2037504705C143065580 @default.
• W2037504705 hasConceptScore W2037504705C181199279 @default.
• W2037504705 hasConceptScore W2037504705C185592680 @default.
• W2037504705 hasConceptScore W2037504705C207583985 @default.
• W2037504705 hasConceptScore W2037504705C23265538 @default.
• W2037504705 hasConceptScore W2037504705C2776580309 @default.
• W2037504705 hasConceptScore W2037504705C2777727519 @default.
• W2037504705 hasConceptScore W2037504705C55493867 @default.
• W2037504705 hasConceptScore W2037504705C69305403 @default.
• W2037504705 hasConceptScore W2037504705C86803240 @default.
• W2037504705 hasIssue "37" @default.
• W2037504705 hasLocation W20375047051 @default.
• W2037504705 hasLocation W20375047052 @default.
• W2037504705 hasOpenAccess W2037504705 @default.
• W2037504705 hasPrimaryLocation W20375047051 @default.
• W2037504705 hasRelatedWork W1436343526 @default.
• W2037504705 hasRelatedWork W1984499992 @default.
• W2037504705 hasRelatedWork W2019388902 @default.
• W2037504705 hasRelatedWork W2023282076 @default.
• W2037504705 hasRelatedWork W2058412019 @default.
• W2037504705 hasRelatedWork W2171825384 @default.
• W2037504705 hasRelatedWork W2463317572 @default.
• W2037504705 hasRelatedWork W2473160238 @default.
• W2037504705 hasRelatedWork W2519012402 @default.
• W2037504705 hasRelatedWork W85650239 @default.
• W2037504705 hasVolume "35" @default.
• W2037504705 isParatext "false" @default.
• W2037504705 isRetracted "false" @default.
• W2037504705 magId "2037504705" @default.
• W2037504705 workType "article" @default.