Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase [PDF]
Nature Communications, 2023 F1 domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit proceeds in 120° steps against a surrounding α3β3 fueled by ATP hydrolysis. How the ATP hydrolysis reactions occurring in three catalytic αβ dimers are coupled to
Atsuki Nakano +3 more
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Elucidating Events within the Black Box of Enzyme Catalysis in Energy Metabolism: Insights into the Molecular Mechanism of ATP Hydrolysis by F1-ATPase [PDF]
Biomolecules, 2023 Oxygen exchange reactions occurring at β-catalytic sites of the FOF1-ATP synthase/F1-ATPase imprint a unique record of molecular events during the catalytic cycle of ATP synthesis/hydrolysis.
Sunil Nath
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Deleting the IF1-like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis [PDF]
Open Biology, 2018 In oxidative phosphorylation, ATP synthases interconvert two forms of free energy: they are driven by the proton-motive force across an energy-transducing membrane to synthesize ATP and displace the ADP/ATP ratio from equilibrium.
Febin Varghese +4 more
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Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1
eLife, 2017 Hsp90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate ‘client’ proteins, facilitating their folding and activating them for biological function.
Daniel Elnatan +5 more
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Defining the role of ATP hydrolysis in mitotic segregation of bacterial plasmids. [PDF]
PLoS Genetics, 2013 Hydrolysis of ATP by partition ATPases, although considered a key step in the segregation mechanism that assures stable inheritance of plasmids, is intrinsically very weak.
Yoan Ah-Seng +3 more
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Molecular Mechanism of ATP Hydrolysis in an ABC Transporter [PDF]
ACS Central Science, 2018 Hydrolysis of nucleoside triphosphate (NTP) plays a key role for the function of many biomolecular systems. However, the chemistry of the catalytic reaction in terms of an atomic-level understanding of the structural, dynamic, and free energy changes ...
Marten Prieß +3 more
semanticscholar +6 more sources
Electron transfer precedes ATP hydrolysis during nitrogenase catalysis [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2013 The biological reduction of N2 to NH3 catalyzed by Mo-dependent nitrogenase requires at least eight rounds of a complex cycle of events associated with ATP-driven electron transfer (ET) from the Fe protein to the catalytic MoFe protein, with each ET ...
S. Duval +7 more
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Structures and mechanisms of actin ATP hydrolysis. [PDF]
Proc Natl Acad Sci U S A, 2022 The major cytoskeleton protein actin undergoes cyclic transitions between the monomeric G-form and the filamentous F-form, which drive organelle transport and cell motility. This mechanical work is driven by the ATPase activity at the catalytic site in the F-form.
Kanematsu Y +14 more
europepmc +4 more sources
Control of ATP hydrolysis in chloroplasts [PDF]
FEBS Letters, 1987 Dark ATP hydrolysis catalysed by the membrane‐bound preactivated thiol‐modified chloroplast ATPase was measured at constant initial ATP concentration and constant initial phosphate potential c ATP/c ADP·cP i which was adjusted by inverse variation of the concentrations of ADP and Pi.
Heinrich Strotmann +2 more
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Rotary mechanism of V/A-ATPases—how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases? [PDF]
Frontiers in Molecular Biosciences, 2023 V/A-ATPase is a rotary molecular motor protein that produces ATP through the rotation of its central rotor. The soluble part of this protein, the V1 domain, rotates upon ATP hydrolysis.
Ken Yokoyama
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