Binding of Phytopolyphenol Piceatannol Disrupts β/γ Subunit Interactions and Rate-limiting Step of Steady-state Rotational Catalysis in Escherichia coli F1-ATPase

Sekiya, Motohiro; Nakamoto, Robert K.; Nakanishi‐Matsui, Mayumi; Futai, Masamitsu

doi:10.1074/jbc.m112.374868

Cited by 22 publications

(23 citation statements)

References 32 publications

(51 reference statements)

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“…Single-site mutations β E E302T, β E D305E, and γR256L that weaken the β E -catch loop/γ-subunit electrostatic interactions dramatically decrease ATPase activity (31). Additional γ-subunit/(αβ) 3 -ring interactions (28,32,(54)(55)(56)(57)(58) may also contribute to the F 1 -ATPase mechanism ( ). Our results are consistent with studies that show that truncation of subunit γ significantly decreases rotation rate.…”

Section: Discussionmentioning

confidence: 99%

Elastic coupling power stroke mechanism of the F ₁ -ATPase molecular motor

Martin

Ishmukhametov

Spetzler

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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The angular velocity profile of the 120° F-ATPase power stroke was resolved as a function of temperature from 16.3 to 44.6 °C using a Δμ = -31.25 at a time resolution of 10 μs. Angular velocities during the first 60° of the power stroke (phase 1) varied inversely with temperature, resulting in negative activation energies with a parabolic dependence. This is direct evidence that phase 1 rotation derives from elastic energy (spring constant, κ = 50·rad). Phase 2 of the power stroke had an enthalpic component indicating that additional energy input occurred to enable the γ-subunit to overcome energy stored by the spring after rotating beyond its 34° equilibrium position. The correlation between the probability distribution of ATP binding to the empty catalytic site and the negative values of the power stroke during phase 1 suggests that this additional energy is derived from the binding of ATP to the empty catalytic site. A second torsion spring (κ = 150·rad; equilibrium position, 90°) was also evident that mitigated the enthalpic cost of phase 2 rotation. The maximum Δ was 22.6 , and maximum efficiency was 72%. An elastic coupling mechanism is proposed that uses the coiled-coil domain of the γ-subunit rotor as a torsion spring during phase 1, and then as a crankshaft driven by ATP-binding-dependent conformational changes during phase 2 to drive the power stroke.

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Section: Discussionmentioning

confidence: 99%

Elastic coupling power stroke mechanism of the F ₁ -ATPase molecular motor

Martin

Ishmukhametov

Spetzler

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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“…We have studied the detailed mechanism of F 1 rotational catalysis by analyzing mutant enzymes, such as ␥M23K and ␤S174F, and inhibitors (ATP␥S and piceatannol) (9,10,13,14,34,36), which extended the duration of the catalytic dwell but not the duration of the 120°rotation. The catalytic dwell was observed more clearly with these mutations or in the presence of these inhibitors.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit

Nakanishi‐Matsui

Sekiya

Yano

et al. 2014

Journal of Biological Chemistry

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Background:The ⑀ subunit inhibits F 1 -ATPase activity. Results: Truncation of helix 2 or a point mutation in loop 2 of the ⑀ subunit decreased its inhibitory effects on subunit rotation. Conclusion: Helix 2 and loop 2 play pivotal roles in inhibitory regulation of F 1 rotational catalysis. Significance: Structure-based studies on the ⑀ subunit function are critical for understanding the mechanism underlying rotational catalysis of ATP synthase.

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“…ATP is synthesized in mitochondria by F0F1 ATP synthase, a multimeric complex consisting of the catalytic F1 sector (a3b3cde) and the trans-membrane proton pathway, the F0 sector (ab2c10). Several phytochemicals, including piceatannol, Qu, RSV, Cur, (−)epigallocatechin gallate, (−)epicatechin gallate, curcumin, genistein, or biochanin, are able to inhibit F0F1 ATPase, both in mitochondria of mammalian cells or in prokaryotic cells [ 19 , 22 , 23 , 34 , 35 ].…”

Section: Mitochondria Oxidative Phosphorylation and Natural Compmentioning

confidence: 99%

Natural Compounds Modulating Mitochondrial Functions

Gibellini

Bianchini

Biasi

et al. 2015

Evidence-Based Complementary and Alternative Medicine

116

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Mitochondria are organelles responsible for several crucial cell functions, including respiration, oxidative phosphorylation, and regulation of apoptosis; they are also the main intracellular source of reactive oxygen species (ROS). In the last years, a particular interest has been devoted to studying the effects on mitochondria of natural compounds of vegetal origin, quercetin (Qu), resveratrol (RSV), and curcumin (Cur) being the most studied molecules. All these natural compounds modulate mitochondrial functions by inhibiting organelle enzymes or metabolic pathways (such as oxidative phosphorylation), by altering the production of mitochondrial ROS and by modulating the activity of transcription factors which regulate the expression of mitochondrial proteins. While Qu displays both pro- and antioxidant activities, RSV and Cur are strong antioxidant, as they efficiently scavenge mitochondrial ROS and upregulate antioxidant transcriptional programmes in cells. All the three compounds display a proapoptotic activity, mediated by the capability to directly cause the release of cytochrome c from mitochondria or indirectly by upregulating the expression of proapoptotic proteins of Bcl-2 family and downregulating antiapoptotic proteins. Interestingly, these effects are particularly evident on proliferating cancer cells and can have important therapeutic implications.

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Binding of Phytopolyphenol Piceatannol Disrupts β/γ Subunit Interactions and Rate-limiting Step of Steady-state Rotational Catalysis in Escherichia coli F1-ATPase

Cited by 22 publications

References 32 publications

Elastic coupling power stroke mechanism of the F ₁ -ATPase molecular motor

Elastic coupling power stroke mechanism of the F ₁ -ATPase molecular motor

Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit

Natural Compounds Modulating Mitochondrial Functions

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Binding of Phytopolyphenol Piceatannol Disrupts β/γ Subunit Interactions and Rate-limiting Step of Steady-state Rotational Catalysis in Escherichia coli F1-ATPase

Cited by 22 publications

References 32 publications

Elastic coupling power stroke mechanism of the F 1 -ATPase molecular motor

Elastic coupling power stroke mechanism of the F 1 -ATPase molecular motor

Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit

Natural Compounds Modulating Mitochondrial Functions

Contact Info

Product

Resources

About

Elastic coupling power stroke mechanism of the F ₁ -ATPase molecular motor

Elastic coupling power stroke mechanism of the F ₁ -ATPase molecular motor