29 Citations
Beyond being an energy supplier, ATP synthase is a sculptor of mitochondrial cristae.
- BiologyBiochimica et biophysica acta. Bioenergetics
- 2022
Facts and Concepts in Cell Compartmentation
- Biology
- 1998
Endomembranes completely enclose diverse compartments in eukaryotic cells that, due to their particular respective complements of enzymes, carry out variable metabolic functions.
ATPase-ATP Synthase and Mitochondrial Pathology
- Biology, Chemistry
- 1999
The F0-Fl structure has been partly resolved and the mechanisms explaining how proton transfer across F0 could induce conformational changes inside Fl that would induce ATP synthesis are elucidated.
Cell death disguised: The mitochondrial permeability transition pore as the c-subunit of the F(1)F(O) ATP synthase.
- BiologyPharmacological research
- 2015
Clostridium pasteurianum F1Fo ATP Synthase: Operon, Composition, and Some Properties
- BiologyJournal of bacteriology
- 2003
The F1Fo complex from C. pasteurianum was activated by thiocyanate, cyanate, or sulfhydryl compounds; inhibited by sulfite, bisulfite, or bicarbonate; and had tolerance to inhibition by dicyclohexylcarbodiimide.
Physiological roles of the mitochondrial permeability transition pore
- BiologyJournal of Bioenergetics and Biomembranes
- 2016
Recent advances in understanding the molecular components of mPTP and its regulatory mechanisms have determined that decreased uncoupling occurs in states of enhanced mitochondrial efficiency; relative closure ofmPTP therefore contributes to cellular functions as diverse as cardiac development and synaptic efficacy.
Expression, purification, crystallization and preliminary X-ray crystallographic studies of a mitochondrial membrane-associated protein Cbs2 from Saccharomyces cerevisiae
- Biology, ChemistryPeerJ
- 2021
A preliminary X-ray crystallographic study was carried out to investigate the structural characteristics of how Saccharomyces cerevisiae Cbs2 tethers cytochrome b mRNA to the mitochondrial inner membrane, and indicated that the biological assembly of CBS2 may be a dimer.
Oxidative phosphorylation supercomplexes and respirasome reconstitution of the colorless alga Polytomella sp.
- Biology, ChemistryBiochimica et biophysica acta. Bioenergetics
- 2018
The Mitochondrial Permeability Transition Pore: Molecular Structure and Function in Health and Disease
- Biology
- 2017
This chapter will discuss recent advances in understanding the molecular components of mPTP, its regulatory mechanisms during cell death, and its function in diseases of the brain.
ISOLATION, SUBFRACTIONATION AND ENZYMATIC ANALYSIS OF COW AND GOAT HEART MITOCHONDRIA
- Biology
- 2018
The mitochondria are a double membrane bound organelle found in eukaryotic cell that contains large number of enzymes involved in diverse activities such as elongation of fatty acids, oxidation of epinephrine and degradation of tryptophan.
References
SHOWING 1-10 OF 17 REFERENCES
Structure at 2.8 Ă‚ resolution of F1-ATPase from bovine heart mitochondria
- ChemistryNature
- 1994
The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Ă… resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
Crystallization of F1-ATPase from bovine heart mitochondria.
- ChemistryJournal of molecular biology
- 1993
Crystals of the F1-ATPase sector of the ATP synthase complex from bovine heart mitochondria have been grown from solutions containing polyethylene glycol 6000. The crystals diffract to 2.9 A…
Mitochondrial ATP synthase. Quaternary structure of the F1 moiety at 3.6 A determined by x-ray diffraction analysis.
- BiologyThe Journal of biological chemistry
- 1991
H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function
- Chemistry, BiologyJournal of bioenergetics and biomembranes
- 1992
A unique class of suppressor mutations identify a transmembrane helix of subunita that is proposed to interact with the bihelical unit of subunitc during proton transport and the role of multiple units of sub unitc in coupling proton translocation to ATP synthesis is considered.
Coupling between catalytic sites and the proton channel in F1F0-type ATPases.
- ChemistryTrends in biochemical sciences
- 1994
Escherichia coli ATP synthase (F-ATPase): catalytic site and regulation of H+ translocation.
- Biology, ChemistryThe Journal of experimental biology
- 1992
Recent results on the Escherichia coli F-ATPase, in particular its catalytic site in the beta subunit and regulation of H+ transport by the gamma subunit are discussed, which suggests that this subunit has an essential role in coupling catalysis with proton translocation.
Functional sites in F1-ATPases: Location and interactions
- Biology, ChemistryJournal of bioenergetics and biomembranes
- 1992
This review focuses on the location and interaction of three functional sites in F1-ATPases, which are catalytic sites, noncatalytic nucleotide-binding sites, and a site that binds inhibitory amphipathic cations which is at an interface of α and β subunits.
One-step purification of Escherichia coli H(+)-ATPase (F0F1) and its reconstitution into liposomes with neurotransmitter transporters.
- Biology, ChemistryThe Journal of biological chemistry
- 1991
Adenosine triphosphatase from rat liver mitochondria. Crystallization and x-ray diffraction studies of the F1-component of the enzyme.
- ChemistryThe Journal of biological chemistry
- 1978