The thermodynamic basis for the partial control of oxidative phosphorylation by the adenine-nucleotide translocator

1983 ◽  
Vol 11 (1) ◽  
pp. 90-91 ◽  
Author(s):  
HANS V. WESTERHOFF ◽  
ALBERT K. GROEN ◽  
RONALD J. A. WANDERS
Keyword(s):  
Oxidative Phosphorylation ◽  
Adenine Nucleotide ◽  
Adenine Nucleotide Translocator ◽  
Partial Control ◽  
Thermodynamic Basis

The function of the adenine nucleotide translocator in the control of oxidative phosphorylation

1990 ◽  
Vol 1018 (2-3) ◽  
pp. 182-184 ◽  
Author(s):  
Ralf Bohnensack ◽  
Frank Norbert Gellerich ◽  
Lorenz Schild ◽  
Wolfgang Kunz
Keyword(s):  
Oxidative Phosphorylation ◽  
Adenine Nucleotide ◽  
Adenine Nucleotide Translocator

scholarly journals Alteration of mitochondrial oxidative phosphorylation in aged skeletal muscle involves modification of adenine nucleotide translocator

2010 ◽  
Vol 1797 (2) ◽  
pp. 143-151 ◽  
Author(s):  
Gilles Gouspillou ◽  
Isabelle Bourdel-Marchasson ◽  
Richard Rouland ◽  
Guillaume Calmettes ◽  
Jean-Michel Franconi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Oxidative Phosphorylation ◽  
Adenine Nucleotide ◽  
Adenine Nucleotide Translocator ◽  
Mitochondrial Oxidative Phosphorylation

scholarly journals A Walk in the Memory, from the First Functional Approach up to Its Regulatory Role of Mitochondrial Bioenergetic Flow in Health and Disease: Focus on the Adenine Nucleotide Translocator

2021 ◽  
Vol 22 (8) ◽  
pp. 4164
Author(s):  
Anna Atlante ◽  
Daniela Valenti
Keyword(s):  
Oxidative Phosphorylation ◽  
Energy Flow ◽  
Adenine Nucleotide ◽  
Physiological State ◽  
Adenine Nucleotide Translocator ◽  
Inner Mitochondrial Membrane ◽  
Cellular Energy ◽  
Health And Disease ◽  
Disease Focus

The mitochondrial adenine nucleotide translocator (ANT) plays the fundamental role of gatekeeper of cellular energy flow, carrying out the reversible exchange of ADP for ATP across the inner mitochondrial membrane. ADP enters the mitochondria where, through the oxidative phosphorylation process, it is the substrate of Fo-F1 ATP synthase, producing ATP that is dispatched from the mitochondrion to the cytoplasm of the host cell, where it can be used as energy currency for the metabolic needs of the cell that require energy. Long ago, we performed a method that allowed us to monitor the activity of ANT by continuously detecting the ATP gradually produced inside the mitochondria and exported in the extramitochondrial phase in exchange with externally added ADP, under conditions quite close to a physiological state, i.e., when oxidative phosphorylation takes place. More than 30 years after the development of the method, here we aim to put the spotlight on it and to emphasize its versatile applicability in the most varied pathophysiological conditions, reviewing all the studies, in which we were able to observe what really happened in the cell thanks to the use of the “ATP detecting system” allowing the functional activity of the ANT-mediated ADP/ATP exchange to be measured.

scholarly journals Mobilization of Adenine Nucleotide Translocators as Molecular Bases of the Biochemical Threshold Effect Observed in Mitochondrial Diseases

2004 ◽  
Vol 279 (19) ◽  
pp. 20411-20421 ◽  
Author(s):  
Benjamin Faustin ◽  
Rodrigue Rossignol ◽  
Christophe Rocher ◽  
Giovanni Bénard ◽  
Monique Malgat ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Conformational Changes ◽  
Adenine Nucleotide ◽  
Mitochondrial Diseases ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Threshold Effect ◽  
Adenine Nucleotide Translocator ◽  
Flux Increase ◽  
Molecular Bases

The existence of a biochemical threshold effect in the metabolic expression of oxidative phosphorylation deficiencies has considerable implications for the understanding of mitochondrial bioenergetics and the study of mitochondrial diseases. However, the molecular bases of this phenomenon remain unclear. We report here a new mechanism to explain this threshold effect, based on a reserve of enzymes not initially participating in the respiratory rate that can be activated either to respond to a flux increase or to compensate for a defect induced by a mutation. We show that this mobilization occurs through 1) the assembly of inactive adenine nucleotide translocator isoform 1 subunits into oligomeric active carriers or 2) conformational changes in the adenine nucleotide translocator isoform 1 in a permeability transition pore-like structure. We discuss how these transitions are sensitive to the steady state of oxidative phosphorylation functioning or tissue and analyze their consequences on the threshold effect.

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