Piericidin A: A new inhibitor of mitochondrial electron transport

Hall, Carole; Wu, Miji; Crane, F.L.; Takahashi, Hiroaki; Tamura, Saburo; Folkers, Karl

doi:10.1016/0006-291x(66)90214-2

Cited by 80 publications

(37 citation statements)

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“…Piericidins were first reported in the 1960s as insecticides and inhibitors of mitochondrial electron transport (25). Later, the piericidin derivative Mer-A 2026B was discovered and proposed to have vasodilator activity (22,23).…”

Section: Discussionmentioning

confidence: 99%

“…We identified one compound as the piericidin derivative Mer-A 2026B and the other as piericidin A1 (22)(23)(24). Piericidins have previously characterized activity as insecticides, vasodilators, and inhibitors of the mitochondrial NADH dehydrogenase and as general antibiotics against certain bacteria (22,23,(25)(26)(27).…”

Section: Screen To Identify T3ss Inhibitorsmentioning

confidence: 99%

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An NF-κB-Based High-Throughput Screen Identifies Piericidins as Inhibitors of the Yersinia pseudotuberculosis Type III Secretion System

Duncan

Wong

Dupzyk

et al. 2014

Antimicrob Agents Chemother

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Section: Discussionmentioning

confidence: 99%

Section: Screen To Identify T3ss Inhibitorsmentioning

confidence: 99%

An NF-κB-Based High-Throughput Screen Identifies Piericidins as Inhibitors of the Yersinia pseudotuberculosis Type III Secretion System

Duncan

Wong

Dupzyk

et al. 2014

Antimicrob Agents Chemother

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“…It has been proposed that the action of piericidin A in the NADH flavin region is exerted in a rotenone like manner [5]. Moreover, it has recently been shown that the binding of 1 4 C labelled rotenone to submitochondrial particles is decreased in the presence of piericidin A or amytal and hence, the three inhibitors were assumed to compete for the same binding site [29].…”

Section: Discussionmentioning

confidence: 99%

“…It acts as a competitive inhibitor of mitochondrial reactions where coenzyme Q is involved [4,5]. This effect, suggested by a similarity in structure between the quinoid coenzyme and the insecticide, was demonstrated as a release of piericidin A inhibited succinic oxidase by the addition of coenzyme Q.…”

mentioning

confidence: 98%

“…Piericidin A is an insecticidal metabolite of Streptomyces mobarensis, the chemical structure of which has been determined as a pyridine ring with methoxyl groups, nuclear methyl and hydroxyl groups and an isoprenoid-like side chain arranged in a coenzyme Q like manner [ 1 -31. It acts as a competitive inhibitor of mitochondrial reactions where coenzyme Q is involved [4,5]. This effect, suggested by a similarity in structure between the quinoid coenzyme and the insecticide, was demonstrated as a release of piericidin A inhibited succinic oxidase by the addition of coenzyme Q.…”

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The Effect of Piericidin A on Energy‐Linked Processes in Submitochondrial Particles

Vallin

Löw

1968

European Journal of Biochemistry

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1. Piericidin A inhibits the oxidative phosphorylation capacity of the NADH oxidase in submitochondrial systems a t concentrations of 30 pmoles/mg protein, that of the succinic oxidase at 6 nmoles/mg protein and the phosphorylation in the cytochrome oxidase region a t concentrations of 5 vmoles/mg protein.2. The energy dependent NAD' reductions are 10 times more sensitive to piericidin A than the NADH oxidase reaction. There is a correlation between the oxidation reduction state of the respiratory chain components, presumably of coenzyme Q and the extent of sensivity to the inhibitor.3. Piericidin A and guanidine compounds showed an additive or more than additive inhibitory effect when added together.4. p-Chloromercuribenzoate and piericidin have a synergistic effect when added simultaneously. 2,3-Dimercaptopropanol (BAL) could partly release the piericidin inhibition, in contrast to glutathione, indicating an involvement of proximal -SH-groups in the piericidin sensitive site.5. Some discrepancies between the piericidin action and the inhibitory action of rotenone and amytal are noted.6. A hypothesis is put forward for the possible interaction of a non-heme iron component, structurally arranged by S-bonds and coenzyme Q and the relevance of this chelate for the generation of a primary high energy complex.Piericidin A is an insecticidal metabolite of Streptomyces mobarensis, the chemical structure of which has been determined as a pyridine ring with methoxyl groups, nuclear methyl and hydroxyl groups and an isoprenoid-like side chain arranged in a coenzyme Q like manner [ 1 -31.It acts as a competitive inhibitor of mitochondrial reactions where coenzyme Q is involved [4,5]. This effect, suggested by a similarity in structure between the quinoid coenzyme and the insecticide, was demonstrated as a release of piericidin A inhibited succinic oxidase by the addition of coenzyme Q. It was further shown that NADH oxidase was sensitive to extremely low concentrations of piericidin A.The reduction of cytochrome b after addition of NADH or succinate is considerably delayed in the presence of piericidin A and coenzyme Q reduction is completely abolished (61.

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Development of Glucose Transporter (GLUT) Inhibitors

Reckzeh

Waldmann

2019

Eur J Org Chem

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The discovery of novel compound classes endowed with biological activity is at the heart of chemical biology and medicinal chemistry research. This enables novel biological insights and inspires new approaches to the treatment of diseases. Cancer cells frequently exhibit altered glycolysis and glucose metabolism and an increased glucose demand. Thus, targeting glucose uptake and metabolism may open up novel opportunities for the discovery of compounds that differentiate [a]

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Piericidin A: A new inhibitor of mitochondrial electron transport

Cited by 80 publications

References 6 publications

An NF-κB-Based High-Throughput Screen Identifies Piericidins as Inhibitors of the Yersinia pseudotuberculosis Type III Secretion System

An NF-κB-Based High-Throughput Screen Identifies Piericidins as Inhibitors of the Yersinia pseudotuberculosis Type III Secretion System

The Effect of Piericidin A on Energy‐Linked Processes in Submitochondrial Particles

Development of Glucose Transporter (GLUT) Inhibitors

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