Oxidation and reduction of exogenous cytochrome c by the activity of the respiratory chain

Lofrumento, N.E.; Marzulli, Domenico; Cafagno, L.; Piana, Gianluigi La; Cipriani, Thales R.

doi:10.1016/0003-9861(91)90198-r

Cited by 23 publications

(23 citation statements)

References 19 publications

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“…It should be noted that, as debated by others, there is significant controversy over the presence of LDH within pure mitochondria and the existence of a lactate shuttle in skeletal muscle mitochondria (16,20,59,147,156,184). In recent years, the NADH/ cytochrome c (Cyto c) electron transport shuttle has also been described, in which the direct transfer of electrons from cytosolic NADH to molecular oxygen inside the mitochondrial matrix is achieved at respiratory contact sites (i.e., where both mitochondrial membranes are in contact) (1,123). The transfer capacity of the NADH/Cyto c is reported to be equivalent to the M-A shuttle (1,123).…”

Section: Shuttling Of Nadh Into the Mitochondriamentioning

confidence: 99%

“…In recent years, the NADH/ cytochrome c (Cyto c) electron transport shuttle has also been described, in which the direct transfer of electrons from cytosolic NADH to molecular oxygen inside the mitochondrial matrix is achieved at respiratory contact sites (i.e., where both mitochondrial membranes are in contact) (1,123). The transfer capacity of the NADH/Cyto c is reported to be equivalent to the M-A shuttle (1,123). However, whether this system is active in skeletal muscle mitochondria, or is regulated by exercise training, is unknown.…”

Section: Shuttling Of Nadh Into the Mitochondriamentioning

confidence: 99%

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NAD⁺/NADH and skeletal muscle mitochondrial adaptations to exercise

White

Schenk

2012

American Journal of Physiology-Endocrinology and Metabolism

151

139

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The pyridine nucleotides, NAD+and NADH, are coenzymes that provide oxidoreductive power for the generation of ATP by mitochondria. In skeletal muscle, exercise perturbs the levels of NAD+, NADH, and consequently, the NAD+/NADH ratio, and initial research in this area focused on the contribution of redox control to ATP production. More recently, numerous signaling pathways that are sensitive to perturbations in NAD+(H) have come to the fore, as has an appreciation for the potential importance of compartmentation of NAD+(H) metabolism and its subsequent effects on various signaling pathways. These pathways, which include the sirtuin (SIRT) proteins SIRT1 and SIRT3, the poly(ADP-ribose) polymerase (PARP) proteins PARP1 and PARP2, and COOH-terminal binding protein (CtBP), are of particular interest because they potentially link changes in cellular redox state to both immediate, metabolic-related changes and transcriptional adaptations to exercise. In this review, we discuss what is known, and not known, about the contribution of NAD+(H) metabolism and these aforementioned proteins to mitochondrial adaptations to acute and chronic endurance exercise.

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Section: Shuttling Of Nadh Into the Mitochondriamentioning

confidence: 99%

Section: Shuttling Of Nadh Into the Mitochondriamentioning

confidence: 99%

NAD⁺/NADH and skeletal muscle mitochondrial adaptations to exercise

White

Schenk

2012

American Journal of Physiology-Endocrinology and Metabolism

151

139

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“…The idea that the OMM rupture might relate to the aging mechanisms was also recently suggested by Skulachev (21). According to some data, the rate of external NADH oxidation by rat liver mitochondria may be stimulated by extramitochondrial cytochrome c (22). The concept of "bi-trans-membrane" electron transport was developed to explain this phenomenon (22)(23)(24), assuming its possible relation to the mechanisms of apoptosis (25).…”

mentioning

confidence: 95%

“…According to some data, the rate of external NADH oxidation by rat liver mitochondria may be stimulated by extramitochondrial cytochrome c (22). The concept of "bi-trans-membrane" electron transport was developed to explain this phenomenon (22)(23)(24), assuming its possible relation to the mechanisms of apoptosis (25). These authors suggested that extramitochondrial cytochrome c, reduced on the OMM by external NADH, might be directly oxidized by cytochrome c oxidase of mitochondria, transferring electrons through the intact OMM.…”

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confidence: 99%

Cytochrome c Sorption-Desorption Effects on the External NADH Oxidation by Mitochondria

Lemeshko

2002

Journal of Biological Chemistry

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The rupture of the outer mitochondrial membrane is known to be critical for cell death, but the mechanism, specifically its redox-signaling aspects, still needs to be studied in more detail. In this work, the external NADH oxidation by rat liver mitochondria was studied under the outer membrane rupture induced by the mitochondria hypotonic treatment or the inner membrane permeability transition. The saturation of the oxidation rate was observed as a function of mitochondrial protein concentration. This effect was shown to result from cytochrome c binding to the mitochondrial membranes. At a relatively high concentration of mitochondria, the oxidation rate was strongly activated by 4 mM Mg 2؉ due to cytochrome c desorption from the membranes. A minimal kinetic model was developed to explain the main phenomena of the external NADH oxidation modulated by cytochrome c and Mg 2؉ in mitochondria with the ruptured outer membrane. The computational behavior of the model closely agreed with the experimental data. We suggest that the redox state of the released cytochrome c, considered by other authors to be important for apoptosis, may strongly depend on its oxidation by the fraction of mitochondria with the ruptured outer membrane and on the cytoplasmic cytochrome c reductase activity.

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“…The reaction was then triggered by the addition of 5 mM succinate. After 2 min, 6 µM myxothiazol was added to account for complex IIIindependent reduction of cytochrome c (Lofrumento et al, 1991).…”

Section: Succinate-cytochrome C Oxidoreductasementioning

confidence: 99%

Hepatopancreas mitochondria of Mytilus galloprovincialis: effect of zinc ions on mitochondrial bioenergetics and metabolism

Lisi¹,

Prato²,

Biandolino³

et al. 2013

Turk J Biol

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Oxygen uptake, respiratory complexes, and metabolic activities have been studied in mitochondria isolated from the hepatopancreata of Mytilus galloprovincialis collected in the "Mar Grande" of Taranto (Ionian Sea, Italy). Although exposure to 5.0 µg Zn 2+ /L resulted in a significant increase of states 3 and 4 respiration with glutamate + pyruvate as respiratory substrate, it was found that the exposure of mussels to different concentrations of Zn 2+ (2.5-7.5 µg/L) neither inhibited mitochondrial respiration nor exerted any inhibitory effect on representative mitochondrial dehydrogenases. It rather stimulates these activities, producing an extra synthesis of adenosine triphosphate by hepatopancreas mitochondria and possibly increasing its availability in the cytoplasmic compartment. This might be considered as a specific strategy utilized by the mussel to cope with variations in the heavy metals content of the marine environment, and it could be used to detect toxic effects.

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Oxidation and reduction of exogenous cytochrome c by the activity of the respiratory chain

Cited by 23 publications

References 19 publications

NAD⁺/NADH and skeletal muscle mitochondrial adaptations to exercise

NAD⁺/NADH and skeletal muscle mitochondrial adaptations to exercise

Cytochrome c Sorption-Desorption Effects on the External NADH Oxidation by Mitochondria

Hepatopancreas mitochondria of Mytilus galloprovincialis: effect of zinc ions on mitochondrial bioenergetics and metabolism

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Oxidation and reduction of exogenous cytochrome c by the activity of the respiratory chain

Cited by 23 publications

References 19 publications

NAD+/NADH and skeletal muscle mitochondrial adaptations to exercise

NAD+/NADH and skeletal muscle mitochondrial adaptations to exercise

Cytochrome c Sorption-Desorption Effects on the External NADH Oxidation by Mitochondria

Hepatopancreas mitochondria of Mytilus galloprovincialis: effect of zinc ions on mitochondrial bioenergetics and metabolism

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NAD⁺/NADH and skeletal muscle mitochondrial adaptations to exercise

NAD⁺/NADH and skeletal muscle mitochondrial adaptations to exercise