Thermodynamic Relationships in Mitochondrial Oxidative Phosphorylation

Wilson, David F.; Erecińska, Maria; Dutton, P. Leslie

doi:10.1146/annurev.bb.03.060174.001223

Cited by 86 publications

(33 citation statements)

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“…This reaction is readily reversible, and NAD ϩ can be reduced using reducing equivalents from reduced cytochrome c when ATP is added to isolated mitochondria (13,32,56,68). The reported intrachain electron transfer rates, expressed as cytochrome c turnover numbers, are Ͼ1,000 s Ϫ1 (5,17), and that is more than 100 times the net rate of electron transfer rates observed in resting cells.…”

Section: Resultsmentioning

confidence: 99%

“…The reported intrachain electron transfer rates, expressed as cytochrome c turnover numbers, are Ͼ1,000 s Ϫ1 (5,17), and that is more than 100 times the net rate of electron transfer rates observed in resting cells. For these and other reasons (10,13,66,68,75), the first two sites can be considered near equilibrium under cellular conditions. The equilibrium constant for reaction shown in Eq.…”

Section: Resultsmentioning

confidence: 99%

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Programming and regulation of metabolic homeostasis

Wilson

2015

American Journal of Physiology-Endocrinology and Metabolism

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Wilson DF. Programming and regulation of metabolic homeostasis. Am J Physiol Endocrinol Metab 308: E506 -E517, 2015. First published January 20, 2015 doi:10.1152 doi:10. /ajpendo.00544.2014dence is presented that the rate and equilibrium constants in mitochondrial oxidative phosphorylation set and maintain metabolic homeostasis in eukaryotic cells. These internal constants determine the energy state ([ATP]/[ADP][P i]), and the energy state maintains homeostasis through a bidirectional sensory/signaling control network that reaches every aspect of cellular metabolism. The energy state is maintained with high precision (to ϳ1 part in 10 10 ), and the control system can respond to transient changes in energy demand (ATP utilization) of more than 100 times the resting rate. Epigenetic and environmental factors are able to "fine-tune" the programmed set point over a narrow range to meet the special needs associated with cell differentiation and chronic changes in metabolic requirements. The result is robust across-platform control of metabolism, which is essential to cellular differentiation and the evolution of complex organisms. A model of oxidative phosphorylation is presented, for which the steady-state rate expression has been derived and computer programmed. The behavior of oxidative phosphorylation predicted by the model is shown to fit the experimental data available for isolated mitochondria as well as for cells and tissues. This includes measurements from several different mammalian tissues as well as from insect flight muscle and plants. The respiratory chain and oxidative phosphorylation is remarkably similar for all higher plants and animals. This is consistent with the efficient synthesis of ATP and precise control of metabolic homeostasis provided by oxidative phosphorylation being a key to cellular differentiation and the evolution of structures with specialized function. oxygen; oxidative phosphorylation; energy metabolism; oxygen pressure; metabolic control; mitochondria; respiratory control THOUSANDS OF DIFFERENT METABOLITES AND ENZYMES must work together if a cell is to survive and grow. In addition to the complex ensemble of reactions within individual cells, in organisms with extensive cellular differentiation, metabolism must support the robust cell-to-cell communication needed for different cell types to contribute to integrated function of the organism. DNA contains the blueprint needed to construct the parts of the ensemble, but in living cells metabolism has to constantly and rapidly respond to changes in the environment. These metabolic responses often occur in seconds, far faster than information encoded in the DNA can be read and implemented. Real-time control of metabolism requires a metabolic unit with intrinsic properties that drive it toward a particular metabolic condition (set point) and is connected to the rest of metabolism through a network of regulatory pathways that maintain that set point (65). To control the ensemble, this central control unit needs to have sensory input fr...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Programming and regulation of metabolic homeostasis

Wilson

2015

American Journal of Physiology-Endocrinology and Metabolism

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“…Anaerobic potentiometric titrations were carried out as described by D&ton [28] and Wilson and Dutton [29] . At the desired oxidation-reduction potential values, the aliquots were transferred anaerobically to 1 mm i.d.…”

Section: Methodsmentioning

confidence: 99%

Spectral evidence for interactions between membrane‐bound hemes: Resonance Raman spectra of mitochondrial cytochrome b–c₁ complex as a function of redox potential

Adar¹,

Erecińska²

1977

FEBS Letters

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“…However, it is still unclear how changes in transport rate elicit corresponding alterations in aerobic respiration. Attempts to answer this question have focused on the role of the cellular concentrations of ATP, ADP, and orthophosphate (Pi), or a combination of these variables to express a phosphate potential (7,8) or energy charge (9), in controlling the mitochondrial respiratory rate. In theory, an increase in active ion transport would cause an increase in the rate of ATP hydrolysis, which would be expected to elicit a decrease in the cellular concentration of ATP and an increase in the concentration of the ATP hydrolysis products, ADP and P1.…”

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Coupling of active ion transport and aerobic respiratory rate in isolated renal tubules.

Balaban¹,

Mandel²,

Soltoff³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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We report the results of studies in which the cytoplasmic coupling between Na+,K+-ATPase activity (presumably a measure of active transport) and the mitochondrial respiratory rate was investigated in a tubule suspension from the rabbit kidney cortex. Simultaneous measurements of the redox state of mitochondrial nicotinamide adenine dinucleotide (NAD) (performed fluorometrically), the cellular ATP and ADP concentrations, and the oxygen consumption rate (Qo) were made under conditions known to alter the Na+,K+-ATPase turnover. Ouabain (25 AM) caused: (i) a 54% inhibition of Qo2,(ii) a net reduction of NAD, and (iii) a 30% increase in the ATP/ADP ratio. The addition of K+ (5 mM) to K+-depleted tubules caused: (i) an initial 127% stimulation of Qo2 followed by a new steady-state Qo2 50% above control, (ii) an initial large oxidation of NAD followed by a new steady state more oxidized than the control level, and (iii) a 47% decrease in the cellular ATP/ADP ratio. These data indicate that the cellular ATP and ADP concentrations or the ATP/ADP ratio may be part of the coupling mechanism linking Na+,K+-ATPase turnover and the aerobic metabolic rate in kidney.A basic question in cellular physiology concerns the mechanism whereby the rate of aerobic conversion of energy is coupled to the rate of active ion transport. A linear relationship between the rate of oxygen consumption and active sodium transport has been observed in numerous epithelia such as frog skin (1), toad bladder (2), and kidney (3, 4), indicating a close link between these two processes. Because Na+,K+-ATPase appears to be either directly or indirectly involved in most active sodium transport processes (5, 6), it is generally accepted that ATP is the most likely energy source for sodium transport. However, it is still unclear how changes in transport rate elicit corresponding alterations in aerobic respiration. Attempts to answer this question have focused on the role of the cellular concentrations of ATP, ADP, and orthophosphate (Pi), or a combination of these variables to express a phosphate potential (7,8) or energy charge (9), in controlling the mitochondrial respiratory rate. In theory, an increase in active ion transport would cause an increase in the rate of ATP hydrolysis, which would be expected to elicit a decrease in the cellular concentration of ATP and an increase in the concentration of the ATP hydrolysis products, ADP and P1. In a model suggested by Whittam and coworkers (10, 11), such an increase in ADP and Pi concentrations could serve as a cytoplasmic feedback signal resulting in an acceleration of the mitochondrial respiratory rate, as described for isolated mitochondria by Chance and Williams (12). We present here experiments performed on an isolated cortical tubule suspension from the rabbit (21), which is ideally suited to test directly the role of ATP and ADP concentrations and the ATP/ADP ratio in the coupling of cellular respiration to cellular ion transport. This preparation contains little glomerular contamination, is no...

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Thermodynamic Relationships in Mitochondrial Oxidative Phosphorylation

Cited by 86 publications

References 30 publications

Programming and regulation of metabolic homeostasis

Programming and regulation of metabolic homeostasis

Spectral evidence for interactions between membrane‐bound hemes: Resonance Raman spectra of mitochondrial cytochrome b–c₁ complex as a function of redox potential

Coupling of active ion transport and aerobic respiratory rate in isolated renal tubules.

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Thermodynamic Relationships in Mitochondrial Oxidative Phosphorylation

Cited by 86 publications

References 30 publications

Programming and regulation of metabolic homeostasis

Programming and regulation of metabolic homeostasis

Spectral evidence for interactions between membrane‐bound hemes: Resonance Raman spectra of mitochondrial cytochrome b–c1 complex as a function of redox potential

Coupling of active ion transport and aerobic respiratory rate in isolated renal tubules.

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Spectral evidence for interactions between membrane‐bound hemes: Resonance Raman spectra of mitochondrial cytochrome b–c₁ complex as a function of redox potential