Mn<sup>2+</sup> inside submitochondrial particles as a tool for studying the functional state of the mitochondrial membrane

Imedidze, E.A.; Drobinskaya, Irina; Kerimov, T.M.; Ruuge, E. K.; Kozlov, I. A.

doi:10.1016/0014-5793(78)81074-6

Cited by 7 publications

(5 citation statements)

References 12 publications

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“…ESR Measurements. ESR spectra of intact S. aureus cells were measured, but we were unable to detect the presence of paramagnetic ions, probably due to binding of the ions to negatively charged ligands (Imedidze et al, 1978). An examination of a cell extract in 6% perchloric acid did reveal a sextet pattern characteristic of free Mn(II) hexaquo ions with g = 2.0090 and a peak to peak distance of 95 G. When the pH of the extract solution was raised with concentrated NaOH, the ESR signal was markedly reduced and barely detectable above pH 6.0.…”

Section: Resultsmentioning

confidence: 90%

“…The presence of Mn(II) ions is very likely the source of line broadening and shifts observed in the 31P and 13C NMR spectra of energydepleted and glycolyzing cells. More importantly, the narrowing line width and upfield shift of the intracellular orthophosphate and lactate resonances whenever the cells are oxygenated suggest that manganese may be involved in oxygen metabolism, either directly or indirectly via changes induced in the intracellular pH (Imedidze et al, 1978; Archibald & Fridovich, 1981a,b). Further studies on the effects of manganese in a variety of microorganisms are currently under way in our laboratory.…”

Section: Discussionmentioning

confidence: 99%

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Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Ezra¹,

Lucas²,

Mustacich³

et al. 1983

Biochemistry

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Section: Resultsmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Ezra¹,

Lucas²,

Mustacich³

et al. 1983

Biochemistry

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“…3 and 6 show that some Ca2+ can be removed by chelators without any effect on the NADH oxidation. Since the outer membrane is permeable to all molecules employed in the present study (Pfaff et al, 1968) and since the mitochondrial inner membrane is not thought to be permeable to EDTA or EGTA (Imedidze et al, 1978;Reed & Bygrave, 1974;Wehrle et al, 1976), addition of chelators in the presence of 9-aminoacridine will yield information on the two surfaces of the outer membrane as well as on the outer surface of the inner membrane, where the NADH dehydrogenase appears to be located (Palmer & Passam, 1971). It is very likely that a portion of the bivalent cations that can be seen by the 9-aminoacridine technique (Figs.…”

Section: Discussionmentioning

confidence: 97%

A specific role for Ca2+ in the oxidation of exogenous NADH by Jerusalem-artichoke (Helianthus tuberosus) mitochondria

Møller¹,

Johnston²,

Palmer³

1981

Biochemical Journal

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1. The addition of chelators to a suspension of mitochondria in a low-cation medium containing 9-aminoacridine caused a decrease in 9-aminoacridine fluorescence. The chelators removed bivalent cations from the membranes and allowed more 9-aminoacridine to move into the diffuse layer. The relative effect of EGTA and EDTA on the fluorescence suggested that the mitochondria are isolated with about equal amounts of Ca2+ and Mg2+ on the membranes. 2. The removal of the bivalent ions by chelators resulted in the inhibition of NADH oxidation. The inhibition could not be removed by adding sufficient decamethylenebistrimethylammonium ion (DM2+) to screen the fixed charges on the membranes and restore the fluorescence of 9-aminoacridine. This observation suggests that bivalent metal ions have a specific role in the oxidation of NADH. 3. Ca2+ and not Mg2+ reversed the inhibition of NADH oxidation caused by EGTA, whereas both reversed the inhibition caused by EDTA. This suggests that Ca2+ plays a specific role and that Mg2+ reverses the inhibition caused by EDTA by displacing the bound calcium from the chelator. 4. The results are interpreted as showing that Ca2+ plays a specific role in the oxidation of external NADH in addition to its ability to screen electrostatically or bind to the fixed charges associated with the surface of the membrane.

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“…An underlying assumption was that the permeability of the SMP was similar to that of the intact mitochondria, i.e. that neither EGTA (Reed and Bygrave 1974, Wehrle et al 1976, Imedidze et al 1978 nor NADH (von Jagow and Kiingenberg 1970) entered vesicles of either polarity. It is, of course, possible that the SMP -resealed inner membrane vesiclesare more 'leaky' after the sonication treatment.…”

Section: Discussionmentioning

confidence: 99%

Direct evidence for the presence of a rotenone‐resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria

Møller

Palmer

1982

Physiologia Plantarum

119

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Meller, I. M. and Palmer, J. M. 1982. Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria. -Physiol. Plant. 54: 267-274.Submitochondrial particles (SMP) were produced from Jerusalem artichoke {Helianlhus tuberosus L.) mitochondria by sonication and differential centrifugation. The SMP were about 50% inside-out as measured by the access of reduced cytochrome c to cytochrome c oxidase. Uncoupled NADH oxidation (1 niM NADH) by the SMP was 120 nmol O2 min'hng~\ which was reduced to 98 nmol O2 min~^ (mg niitochondrial protein)"' in the presence of EGTA. In contrast, the oxidation of NADH by intact mitochondria was completely inhibited by EGTA (from 182 to 14 nmol O2 min*^mg~'). The EGTA-resistant NADH oxidation by the SMP is ascribed to the NADH dehydrogenase(s) on the inside of the inner membrane and exposed to the medium in the inside-out SMP. In the presence of EGTA it could be shown that two NADH dehydrogenase activities were present in the SMP. One had an apparent K^ of 7 nM for NADH, a V"" o.f 80 nmol NADH mio^'mg-^ and was rotenone-sensitive. TMs dehydrogenase is equivalent to the mammalian Complex I NADH dehydrogenase. The other dehydrogenase, which was rotenone-resistant, had a Kn of 80 f UW and a V^j,, of 131 nmol NADH mio^'mg"'; it is probably responsible for the rotenone-resistant oxidation of organic acids often observed io plant mitochondria. The redox poise of the pyridine nucleotides had only a small effect on the relative rates of the two internal dehydrogenases. Electron flow through these dehydrogenases appears, therefore, to be regulated mainly by the concentration of NADH in the matrix of the mitochondria.Additional key-words -Nicotinamide adenine dinucleotide (reduced), pyridine nucleotide, redox poise, submitochondrial particles. /. M. M0l(er (present address and address for reprint requests),

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Mn²⁺ inside submitochondrial particles as a tool for studying the functional state of the mitochondrial membrane

Cited by 7 publications

References 12 publications

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

A specific role for Ca2+ in the oxidation of exogenous NADH by Jerusalem-artichoke (Helianthus tuberosus) mitochondria

Direct evidence for the presence of a rotenone‐resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria

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Mn2+ inside submitochondrial particles as a tool for studying the functional state of the mitochondrial membrane

Cited by 7 publications

References 12 publications

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

A specific role for Ca2+ in the oxidation of exogenous NADH by Jerusalem-artichoke (Helianthus tuberosus) mitochondria

Direct evidence for the presence of a rotenone‐resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria

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Mn²⁺ inside submitochondrial particles as a tool for studying the functional state of the mitochondrial membrane