The site of the action of rotenone in the respiratory chain

Öberg, K.E.

doi:10.1016/0014-4827(61)90263-4

Cited by 61 publications

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“…Furthermore, rotenone is generally considered from the work *on animal tissue and mitochondria to mimic practically all the known features of the amytal effects on the electron transport svstem: both chemicals specifically inhibit the NAD+-linked respiration of mitochondria (7,10,27,28). Ouir re-sults (figs 3 and 4) in general, agree with this concept.…”

supporting

confidence: 76%

“…The difference in 'Ki values between rotenone and amytal witlh animal mitochondria is as much as 4 orders of magnitude. Both chemicals, at high concentrations, apparently inhibit completely NAD -linked substrate respiration (7,10,27,28). These results indicate a 'strong dissimilarity in the action of amytal and rotenone between aniimal and plant mitochondria.…”

mentioning

confidence: 61%

“…The sulmmary of a series of experiments is shown in figure 7A. Rotenone has been claimed to be by far the most potent inhilbitor of the electron transport system of animal mitochondria and its titer value changes lineariy with mitochondrial concentrations (7,10,27,28 4). Clearly this chemical is at least 500 times less effective on mung bean mitochondria than it is otn rat liver mitochondria.…”

mentioning

confidence: 99%

“…Tllhe site of action of amytal alnd rotenone has been identified to be on the substrate side of cvtochrome b (7,28), probably on the substrate side of fla'voprotein (7). Furthermore, rotenone is generally considered from the work *on animal tissue and mitochondria to mimic practically all the known features of the amytal effects on the electron transport svstem: both chemicals specifically inhibit the NAD+-linked respiration of mitochondria (7,10,27,28).…”

mentioning

confidence: 99%

“…Class I inclutdes the classical inhibitor, malonate, which acts as a specific, competitive invhibitor of succinic dehydrogenase. From the wrork on animal mitochondria, the class II inhibitors, amytal and rotenone, are considered to act at the same site in the oxidation of NAD~-linked substrates (7,10,27,28). The site of inhibitory action of antimycin A and 2-alkyl-4-hydroxyquinoline N-oxide has been localized, particularly fromii spectrophotometric observations, betweeln cytochromlie b and cytochrome c of the respiratory chain (1,4,5,8,13,20,26).…”

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confidence: 99%

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Properties of Higher Plant Mitochondria. III. Effects of Respiratory Inhibitors

Ikuma

Bonner

1967

Plant Physiol.

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196{. Summilary. The effects of representative respiratory inhijbitors were ilnvestigated on the coupled respiration of mung bean nitochondria tusing succinate and l-malate as substrates. The inthibitors studied were: (I) mlalonate, (II) The inhibition of respiratory electron transport in both plant and animal mitochondria has been shown repeatedly !to be achieved bv the following 4 classes of inhibitors (cf. 9,12, 15, and (IV) inhibitors of cytochrome c oxidase. Class I inclutdes the classical inhibitor, malonate, which acts as a specific, competitive invhibitor of succinic dehydrogenase. From the wrork on animal mitochondria, the class II inhibitors, amytal and rotenone, are considered to act at the same site in the oxidation of NAD~-linked substrates (7,10,27,28). The site of inhibitory action of antimycin A and 2-alkyl-4-hydroxyquinoline N-oxide has been localized, particularly fromii spectrophotometric observations, betweeln cytochromlie b and cytochrome c of the respiratory chain (1,4,5,8,13,20,26). Cyanide and azide are among the classical inhibitors of cytochrome oxidase (16,21,22,31,(34)(35)(36)38

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confidence: 76%

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confidence: 61%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Properties of Higher Plant Mitochondria. III. Effects of Respiratory Inhibitors

Ikuma

Bonner

1967

Plant Physiol.

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The DPNH Dehydrogenase of the Mitochondrial Respiratory Chain

Singer¹,

Gutman²

1971

Advances in Enzymology - And Related Areas of Molecular Biology

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Correlation of increased intraacrosomal pH with the hamster sperm acrosome reaction

Working

Meizel

1983

J. Exp. Zool.

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This study describes investigations of the importance of intraacrosomal pH in the hamster sperm acrosome reaction (AR). Washed cauda epididymal sperm were capacitated in vitro in a medium containing 2 mM Ca2+, 144 mM Na+, and 3 mM K+. Such sperm underwent a significant increase in the number of AR within 10 min after the addition of the Mg2+-ATPase (adenosine triphosphatase) inhibitors DCCD (20 microM) or NBD-Cl (10 microM) or the proton ionophore FCCP (6 micrograms/ml) at 3.5 hr of incubation or after addition of HN4Cl (3 mM) at 4 hr of incubation. Addition of the mitochondrial electron transport inhibitor rotenone (2.5 microM) at 3.5 hr or of NaCl (3 mM) or KCl (3 mM) at 4 hr did not stimulate AR over control levels, suggesting that the stimulation of AR by the other compounds was not directly due to depletion of acrosomal adenosine triphosphate (ATP) or alteration of the acrosomal transmembrane potential. The AR also was not stimulated by either DCCD or FCCP added prior to 3 hr of incubation of sperm, whereas both compounds were increasingly effective at stimulating AR with increasing length of preincubation of sperm before the addition of the test compounds. The intraacrosomal pH of sperm incubated in low [K+] (0.6-0.9 mM) for 3.5 hr rose by at least one pH unit (as measured with the fluorescent dye 9-aminoacridine) within 15-30 min after raising extracellular [K+] to 4.2-4.5 mM. The pH rise occurred even in the presence of the Ca2+-chelator EGTA (2 mM). Either FCCP (8 micrograms/ml) or DCCD (20 microM), but not rotenone (2.5 microM), plus K+ (3.6 mM), raised the intraacrosomal pH of sperm incubated for 3 hr in low [K+] within 10 min after addition. No pH rise occurred in the absence of additional K+. These results demonstrate that the intraacrosomal pH of the hamster sperm becomes more alkaline in a process not requiring high concentrations of external Ca2+, but requiring K+. The results of this and previous studies lead us to suggest here that the intraacrosomal pH rise may be mediated via a change in K+ and H+ permeability of sperm head membranes, which allows K+ influx and H+ efflux, and via inhibition of an acrosomal Mg2+-ATPase proton pump. We propose that the permeability changes and the consequent alkalinization of the acrosomal interior are important steps in late capacitation and/or the mammalian AR.

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The site of the action of rotenone in the respiratory chain

Cited by 61 publications

References 1 publication

Properties of Higher Plant Mitochondria. III. Effects of Respiratory Inhibitors

Properties of Higher Plant Mitochondria. III. Effects of Respiratory Inhibitors

The DPNH Dehydrogenase of the Mitochondrial Respiratory Chain

Correlation of increased intraacrosomal pH with the hamster sperm acrosome reaction

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