Structure and mechanisms of F-type ATP synthases
W Kühlbrandt - Annual review of biochemistry, 2019 - annualreviews.org
F1Fo ATP synthases produce most of the ATP in the cell. F-type ATP synthases have been
investigated for more than 50 years, but a full understanding of their molecular mechanisms …
investigated for more than 50 years, but a full understanding of their molecular mechanisms …
CryoEM reveals the complexity and diversity of ATP synthases
GM Courbon, JL Rubinstein - Frontiers in Microbiology, 2022 - frontiersin.org
During respiration, adenosine triphosphate (ATP) synthases harness the electrochemical
proton motive force (PMF) generated by the electron transport chain (ETC) to synthesize …
proton motive force (PMF) generated by the electron transport chain (ETC) to synthesize …
Structure of the dimeric ATP synthase from bovine mitochondria
TE Spikes, MG Montgomery… - Proceedings of the …, 2020 - National Acad Sciences
The structure of the dimeric ATP synthase from bovine mitochondria determined in three
rotational states by electron cryo-microscopy provides evidence that the proton uptake from …
rotational states by electron cryo-microscopy provides evidence that the proton uptake from …
Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling
INTRODUCTION Mitochondrial F1-Fo adenosine triphosphate (ATP) synthases are
macromolecular turbines that couple proton translocation across a membrane to ATP …
macromolecular turbines that couple proton translocation across a membrane to ATP …
Structure of the human ATP synthase
Y Lai, Y Zhang, S Zhou, J Xu, Z Du, Z Feng, L Yu… - Molecular Cell, 2023 - cell.com
Biological energy currency ATP is produced by F 1 F o-ATP synthase. However, the
molecular mechanism for human ATP synthase action remains unknown. Here, we present …
molecular mechanism for human ATP synthase action remains unknown. Here, we present …
Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
F1Fo ATP synthase functions as a biological rotary generator that makes a major
contribution to cellular energy production. It comprises two molecular motors coupled …
contribution to cellular energy production. It comprises two molecular motors coupled …
Changes within the central stalk of E. coli F1Fo ATP synthase observed after addition of ATP
F1Fo ATP synthase functions as a biological generator and makes a major contribution to
cellular energy production. Proton flow generates rotation in the Fo motor that is transferred …
cellular energy production. Proton flow generates rotation in the Fo motor that is transferred …
Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases
J Kishikawa, A Nakanishi, A Nakano, S Saeki… - Nature …, 2022 - nature.com
V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with FoF1
ATP synthase. When powered by ATP hydrolysis, the V1 domain rotates the central rotor …
ATP synthase. When powered by ATP hydrolysis, the V1 domain rotates the central rotor …
Beyond binding change: the molecular mechanism of ATP hydrolysis by F1-ATPase and its biochemical consequences
S Nath - Frontiers in Chemistry, 2023 - frontiersin.org
F1-ATPase is a universal multisubunit enzyme and the smallest-known motor that, fueled by
the process of ATP hydrolysis, rotates in 120o steps. A central question is how the …
the process of ATP hydrolysis, rotates in 120o steps. A central question is how the …
Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes
TE Spikes, MG Montgomery… - Proceedings of the …, 2021 - National Acad Sciences
The ATP synthase complexes in mitochondria make the ATP required to sustain life by a
rotary mechanism. Their membrane domains are embedded in the inner membranes of the …
rotary mechanism. Their membrane domains are embedded in the inner membranes of the …