Journal ArticleDOI
Mg2+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F1
TLDR
It is concluded that Mg2+-induced inhibition of the ATPase activity of F1 is due to the formation of an inactive F1, and unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1979-08-28. It has received 58 citations till now. The article focuses on the topics: Calcium ATPase & ATPase.read more
Citations
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Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition
Massimo Bonora,Mariusz R. Wieckowski,Christos Chinopoulos,Oliver Kepp,Guido Kroemer,Lorenzo Galluzzi,Paolo Pinton +6 more
TL;DR: Recent findings suggest that another of its core components is represented by the c subunit of mitochondrial ATP synthase, the supramolecular entity that is believed to mediate MPT.
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ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas
Sangjin Hong,Peter L. Pedersen +1 more
TL;DR: The rich source of ATP synthase inhibitors and their known or purported sites of action presented in this review should provide valuable insights into their applications as potential scaffolds for new therapeutics for human and animal diseases as well as for the discovery of new pesticides and herbicides to help protect the world's food supply.
Journal ArticleDOI
Calcium activation of heart mitochondrial oxidative phosphorylation: rapid kinetics of mVO2, NADH, AND light scattering.
TL;DR: Estimates of Ca2+ uptake into mitochondria using opticalCa2+ indicators trapped in the matrix revealed a sufficiently rapid uptake to cause the metabolic effects observed, consistent with the notion that extramitochondrial Ca 2+ can modify ATP production, via an increase in matrix Ca2- content, rapidly enough to support cardiac work transitions in vivo.
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Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite.
TL;DR: The results obtained suggest that the inhibiting effect of azide on mitochondrial ATPase is due to stabilization of inactive E*.ADP complex formed during ATP hydrolysis; the activation of ATPase by sulphite is also realized through the equilibrium between intermediate active E.ADp complex and inactive E *.ADPcomplex.
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Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1-ATPase, is located at the catalytic site of the enzyme
TL;DR: It is proposed that ATP‐dependent dissociation of the F1‐ATPase‐GDP complex occurs more rapidly, than that of the MgADP‐Pi complex, because of the higher rate of ATP hydrolysis.
References
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Journal ArticleDOI
Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation XIII. STRUCTURE AND FUNCTION OF SUBMITOCHONDRIAL PARTICLES COMPLETELY RESOLVED WITH RESPECT TO COUPLING FACTOR 1
TL;DR: Reconstituted SU-particles catalyzed oxidative phosphorylation with a P:O ratio of 0.5 and were morphologically indistinguishable from untreated submitochondrial particles, indicating that coupling factor 1 is responsible for most, if not all, of the inner membrane spheres.
Journal ArticleDOI
An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions.
C Kayalar,J Rosing,Paul D. Boyer +2 more
TL;DR: The Pi in equilibrium ATP exchange is not inhibited by increase in MgADP and MgATP at constant ratios, and the energy-linked ADP in equilibrium ATM exchange isNot inhibited by increased concentrations of M gATP and Pi at a constant ratio, which indicates a random binding and release of ADP andPi.
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Interaction of adenine nucleotides with multiple binding sites on beef heart mitochondrial adenosine triphosphatase.
N E Garrett,H S Penefsky +1 more
TL;DR: Reconstitution of F1 with ADP or with almost 5 mol of AMP-P(NH)P resulted in preparations that exhibited an undiminished capacity to restore oxidative phosphorylation in F1-deficient submitochondrial particles.
Journal ArticleDOI
Tight binding of adenine nucleotides to beef-heart mitochondrial ATPase.
TL;DR: Mitochondrial ATPase (F1) isolated from beef heart contains 5 moles of tightly bound adenine nucleotide per mole of enzyme—3 moles ATP and 2 moles ADP.
Related Papers (5)
Adenine nucleotide binding sites on beef heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites.
R L Cross,C M Nalin +1 more