FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2080459410> ?p ?o ?g. }

• W2080459410 endingPage "22780" @default.
• W2080459410 startingPage "22771" @default.
• W2080459410 abstract "In observations of single molecule behavior under Vmax conditions with minimal load, the F1 sector of the ATP synthase (F-ATPase) rotates through continuous cycles of catalytic dwells (∼0.2 ms) and 120° rotation steps (∼0.6 ms). We previously established that the rate-limiting transition step occurs during the catalytic dwell at the initiation of the 120° rotation. Here, we use the phytopolyphenol, piceatannol, which binds to a pocket formed by contributions from α and β stator subunits and the carboxyl-terminal region of the rotor γ subunit. Piceatannol did not interfere with the movement through the 120° rotation step, but caused increased duration of the catalytic dwell. The duration time of the intrinsic inhibited state of F1 also became significantly longer with piceatannol. All of the beads rotated at a lower rate in the presence of saturating piceatannol, indicating that the inhibitor stays bound throughout the rotational catalytic cycle. The Arrhenius plot of the temperature dependence of the reciprocal of the duration of the catalytic dwell (catalytic rate) indicated significantly increased activation energy of the rate-limiting step to trigger the 120° rotation. The activation energy was further increased by combination of piceatannol and substitution of γ subunit Met23 with Lys, indicating that the inhibitor and the β/γ interface mutation affect the same transition step, even though they perturb physically separated rotor-stator interactions.Background: The β/γ subunit interactions are critical for rotational catalysis in ATP synthase.Results: Piceatannol increases the activation energy for the rate-limiting transition state.Conclusion: Piceatannol binding and a β/γ subunit interface mutation, although the sites are physically separated, affect the same rate-limiting transition-state step.Significance: Multiple rotor-stator interactions contribute to formation of the transition state. In observations of single molecule behavior under Vmax conditions with minimal load, the F1 sector of the ATP synthase (F-ATPase) rotates through continuous cycles of catalytic dwells (∼0.2 ms) and 120° rotation steps (∼0.6 ms). We previously established that the rate-limiting transition step occurs during the catalytic dwell at the initiation of the 120° rotation. Here, we use the phytopolyphenol, piceatannol, which binds to a pocket formed by contributions from α and β stator subunits and the carboxyl-terminal region of the rotor γ subunit. Piceatannol did not interfere with the movement through the 120° rotation step, but caused increased duration of the catalytic dwell. The duration time of the intrinsic inhibited state of F1 also became significantly longer with piceatannol. All of the beads rotated at a lower rate in the presence of saturating piceatannol, indicating that the inhibitor stays bound throughout the rotational catalytic cycle. The Arrhenius plot of the temperature dependence of the reciprocal of the duration of the catalytic dwell (catalytic rate) indicated significantly increased activation energy of the rate-limiting step to trigger the 120° rotation. The activation energy was further increased by combination of piceatannol and substitution of γ subunit Met23 with Lys, indicating that the inhibitor and the β/γ interface mutation affect the same transition step, even though they perturb physically separated rotor-stator interactions. Background: The β/γ subunit interactions are critical for rotational catalysis in ATP synthase. Results: Piceatannol increases the activation energy for the rate-limiting transition state. Conclusion: Piceatannol binding and a β/γ subunit interface mutation, although the sites are physically separated, affect the same rate-limiting transition-state step. Significance: Multiple rotor-stator interactions contribute to formation of the transition state." @default.
• W2080459410 created "2016-06-24" @default.
• W2080459410 creator A5011017894 @default.
• W2080459410 creator A5013606982 @default.
• W2080459410 creator A5024532915 @default.
• W2080459410 creator A5033495188 @default.
• W2080459410 date "2012-06-01" @default.
• W2080459410 modified "2023-10-17" @default.
• W2080459410 title "Binding of Phytopolyphenol Piceatannol Disrupts β/γ Subunit Interactions and Rate-limiting Step of Steady-state Rotational Catalysis in Escherichia coli F1-ATPase" @default.
• W2080459410 cites W1576285340 @default.
• W2080459410 cites W1593015025 @default.
• W2080459410 cites W1604488369 @default.
• W2080459410 cites W1964051078 @default.
• W2080459410 cites W1964976203 @default.
• W2080459410 cites W1983962372 @default.
• W2080459410 cites W1984061771 @default.
• W2080459410 cites W1984302442 @default.
• W2080459410 cites W1994770876 @default.
• W2080459410 cites W1996931402 @default.
• W2080459410 cites W1997842212 @default.
• W2080459410 cites W2005279566 @default.
• W2080459410 cites W2011781339 @default.
• W2080459410 cites W2012230565 @default.
• W2080459410 cites W2013906099 @default.
• W2080459410 cites W2026587433 @default.
• W2080459410 cites W2027197645 @default.
• W2080459410 cites W2034977221 @default.
• W2080459410 cites W2037998901 @default.
• W2080459410 cites W2040686462 @default.
• W2080459410 cites W2043573823 @default.
• W2080459410 cites W2044013892 @default.
• W2080459410 cites W2047543025 @default.
• W2080459410 cites W2063339521 @default.
• W2080459410 cites W2064598149 @default.
• W2080459410 cites W2071950147 @default.
• W2080459410 cites W2074033410 @default.
• W2080459410 cites W2082544726 @default.
• W2080459410 cites W2084121452 @default.
• W2080459410 cites W2132278019 @default.
• W2080459410 cites W2134780839 @default.
• W2080459410 cites W2140969249 @default.
• W2080459410 doi "https://doi.org/10.1074/jbc.m112.374868" @default.
• W2080459410 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3391159" @default.
• W2080459410 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22582396" @default.
• W2080459410 hasPublicationYear "2012" @default.
• W2080459410 type Work @default.
• W2080459410 sameAs 2080459410 @default.
• W2080459410 citedByCount "20" @default.
• W2080459410 countsByYear W20804594102013 @default.
• W2080459410 countsByYear W20804594102014 @default.
• W2080459410 countsByYear W20804594102015 @default.
• W2080459410 countsByYear W20804594102016 @default.
• W2080459410 countsByYear W20804594102017 @default.
• W2080459410 countsByYear W20804594102018 @default.
• W2080459410 countsByYear W20804594102019 @default.
• W2080459410 countsByYear W20804594102020 @default.
• W2080459410 countsByYear W20804594102022 @default.
• W2080459410 countsByYear W20804594102023 @default.
• W2080459410 crossrefType "journal-article" @default.
• W2080459410 hasAuthorship W2080459410A5011017894 @default.
• W2080459410 hasAuthorship W2080459410A5013606982 @default.
• W2080459410 hasAuthorship W2080459410A5024532915 @default.
• W2080459410 hasAuthorship W2080459410A5033495188 @default.
• W2080459410 hasBestOaLocation W20804594101 @default.
• W2080459410 hasConcept C104292427 @default.
• W2080459410 hasConcept C104317684 @default.
• W2080459410 hasConcept C112243037 @default.
• W2080459410 hasConcept C121332964 @default.
• W2080459410 hasConcept C12554922 @default.
• W2080459410 hasConcept C148898269 @default.
• W2080459410 hasConcept C161790260 @default.
• W2080459410 hasConcept C178790620 @default.
• W2080459410 hasConcept C181199279 @default.
• W2080459410 hasConcept C185592680 @default.
• W2080459410 hasConcept C23265538 @default.
• W2080459410 hasConcept C2776816829 @default.
• W2080459410 hasConcept C2779746291 @default.
• W2080459410 hasConcept C55493867 @default.
• W2080459410 hasConcept C62520636 @default.
• W2080459410 hasConcept C71240020 @default.
• W2080459410 hasConcept C8010536 @default.
• W2080459410 hasConcept C86803240 @default.
• W2080459410 hasConcept C93391505 @default.
• W2080459410 hasConcept C95121573 @default.
• W2080459410 hasConceptScore W2080459410C104292427 @default.
• W2080459410 hasConceptScore W2080459410C104317684 @default.
• W2080459410 hasConceptScore W2080459410C112243037 @default.
• W2080459410 hasConceptScore W2080459410C121332964 @default.
• W2080459410 hasConceptScore W2080459410C12554922 @default.
• W2080459410 hasConceptScore W2080459410C148898269 @default.
• W2080459410 hasConceptScore W2080459410C161790260 @default.
• W2080459410 hasConceptScore W2080459410C178790620 @default.
• W2080459410 hasConceptScore W2080459410C181199279 @default.
• W2080459410 hasConceptScore W2080459410C185592680 @default.
• W2080459410 hasConceptScore W2080459410C23265538 @default.
• W2080459410 hasConceptScore W2080459410C2776816829 @default.
• W2080459410 hasConceptScore W2080459410C2779746291 @default.
• W2080459410 hasConceptScore W2080459410C55493867 @default.

• next