[HTML][HTML] ATP synthase in mycobacteria: special features and implications for a function as drug target
P Lu, H Lill, D Bald - Biochimica et Biophysica Acta (BBA)-Bioenergetics, 2014 - Elsevier
ATP synthase is a ubiquitous enzyme that is largely conserved across the kingdoms of life.
This conservation is in accordance with its central role in chemiosmotic energy conversion, a …
This conservation is in accordance with its central role in chemiosmotic energy conversion, a …
F1FO ATP synthase molecular motor mechanisms
WD Frasch, ZA Bukhari, S Yanagisawa - Frontiers in microbiology, 2022 - frontiersin.org
The F-ATP synthase, consisting of F1 and FO motors connected by a central rotor and the
stators, is the enzyme responsible for synthesizing the majority of ATP in all organisms. The …
stators, is the enzyme responsible for synthesizing the majority of ATP in all organisms. The …
Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase
IF1 is a natural inhibitor protein for mitochondrial FoF1 ATP synthase that blocks catalysis
and rotation of the F1 by deeply inserting its N-terminal helices into F1. A unique feature of …
and rotation of the F1 by deeply inserting its N-terminal helices into F1. A unique feature of …
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 …
Bio-layer interferometry for measuring kinetics of protein-protein interactions and allosteric ligand effects
We describe the use of Bio-layer Interferometry to study inhibitory interactions of subunit ε
with the catalytic complex of Escherichia coli ATP synthase. Bacterial F-type ATP synthase is …
with the catalytic complex of Escherichia coli ATP synthase. Bacterial F-type ATP synthase is …
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 …
Diffusion measurements of swimming enzymes with fluorescence correlation spectroscopy
Conspectus Self-propelled chemical motors are chemically powered micro-or nanosized
swimmers. The energy required for these motors' active motion derives from catalytic …
swimmers. The energy required for these motors' active motion derives from catalytic …
Elucidating Events within the Black Box of Enzyme Catalysis in Energy Metabolism: Insights into the Molecular Mechanism of ATP Hydrolysis by F1-ATPase
S Nath - Biomolecules, 2023 - mdpi.com
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 …
ATPase imprint a unique record of molecular events during the catalytic cycle of ATP …
Cryo-EM reveals distinct conformations of E. coli ATP synthase on exposure to ATP
ATP synthase produces the majority of cellular energy in most cells. We have previously
reported cryo-EM maps of autoinhibited E. coli ATP synthase imaged without addition of …
reported cryo-EM maps of autoinhibited E. coli ATP synthase imaged without addition of …
Enhanced diffusion and oligomeric enzyme dissociation
The concept that catalytic enzymes can act as molecular machines transducing chemical
activity into motion has conceptual and experimental support, but experimental support has …
activity into motion has conceptual and experimental support, but experimental support has …