Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase

King, Tsoo E.; Ohnishi, Tomo̧ko; Winter, Daryl B.; Wu, Joy T.

doi:10.1007/978-1-4684-3270-1_15

Cited by 46 publications

(13 citation statements)

References 70 publications

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“…However, the reduction of artificial electron acceptors such as INT only requires the proximal redox centers in SDH, i.e. the FAD (which is reduced by succinate) and S1, the 2Fe/2S center that is reduced by the FADH 2 and that then reduces INT [80]. The second assay for complex II measured the succinate-dependent reduction of ubiquinone which requires electron flow through all of its redox centers, including the FAD, and the S1 (2Fe-2S) and S3 (3Fe4S) centers [77].…”

Section: Resultsmentioning

confidence: 99%

“…The reduced [2Fe-2S] 1+ cluster N1b from complex I has a g ‖ = 2.03 (2.02 in some species) [108], and reduced S1 of complex II has a g z = 2.025 [86]. However, the ratios of the intensities of g = 1.94 (major) to g = 2.02 (minor) for S1 should be constant under different conditions [80]. Since both our temperature and recovery data show that this ratio is not constant, we do not believe that the g = 2.02 signal can be accounted for by a single species.…”

Section: Discussionmentioning

confidence: 99%

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The pro-oxidant chromium(VI) inhibits mitochondrial complex I, complex II, and aconitase in the bronchial epithelium: EPR markers for Fe–S proteins

Myers

Antholine

Myers

2010

Free Radical Biology and Medicine

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Hexavalent chromium [Cr(VI)] compounds (e.g. chromates) are strong oxidants that readily enter cells where they are reduced to reactive Cr species that also facilitate reactive oxygen species (ROS) generation. Recent studies demonstrated inhibition and oxidation of the thioredoxin system, with greater effects on mitochondrial thioredoxin (Trx2). This implies that Cr(VI)-induced oxidant stress may be especially directed at the mitochondria. Examination of other redox-sensitive mitochondrial functions showed that Cr(VI) treatments that cause Trx2 oxidation in human bronchial epithelial cells also result in pronounced and irreversible inhibition of aconitase, a TCA cycle enzyme that has an iron-sulfur (Fe-S) center that is labile with respect to certain oxidants. The activities of electron transport complexes I and II were also inhibited, whereas complex III was not. Electron paramagnetic resonance (EPR) studies of samples at liquid helium temperature (10 K) showed a strong signal at g = 1.94 that is consistent with the inhibition of electron flow through complexes I and/or II. A signal at g = 2.02 was also observed which is consistent with oxidation of the Fe-S center of aconitase. The g = 1.94 signal was particularly intense and remained after extracellular Cr(VI) was removed, whereas the g = 2.02 signal declined in intensity after Cr(VI) was removed. A similar inhibition of these activities and analogous EPR findings were noted in bovine airways treated ex vivo with Cr(VI). Overall, the data support the hypothesis that Cr(VI) exposure has deleterious effects on a number of redox-sensitive core mitochondrial proteins. The g = 1.94 signal could prove to be an important biomarker for oxidative damage resulting from Cr(VI) exposure. The EPR spectra simultaneously showed signals for Cr(V) and Cr(III) which verify Cr(VI) exposure and its intracellular reductive activation.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The pro-oxidant chromium(VI) inhibits mitochondrial complex I, complex II, and aconitase in the bronchial epithelium: EPR markers for Fe–S proteins

Myers

Antholine

Myers

2010

Free Radical Biology and Medicine

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“…The activity of nicotinamide adenine dinucleotide (NADH) dehydrogenase (Complex I) was measured as described by King and Howard (1967). Activity of SDH (Complex II) was assayed according to the method of King et al (1976). The activity of cytochrome oxidase (Complex IV) was assayed according to the method described by Sottocasa et al (1967).…”

Section: Estimation Of Mitochondrial Respiratory Chain Functionsmentioning

confidence: 99%

Mitochondrial modulators in experimental Huntington’s disease: reversal of mitochondrial dysfunctions and cognitive deficits

Mehrotra

Kanwal

Banerjee

et al. 2015

Neurobiology of Aging

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“…The corpus striatum was dissected, rinsed in isotonic saline and mitochondria were isolated by the method described by Stahl et al (1963). Briefly, striatum was homogenized in ice-cold buffer A [10 mM Tris-HCl (pH 7.4), 0.44 M Sucrose, 10 mM EDTA and 0.1% BSA] and centrifuged at 2100g for 15 min at 4 C. The pellet was discarded and the supernatant was further centrifuged at 14,000g for 15 min at 4 C. The crude mitochondrial pellet was separated and washed with buffer A and again spun at 7000g for 15 min at 4 C. The final mitochondrial pellet was resuspended in buffer B [10 mM Tris-HCl (pH 7.4), 0.44 M sucrose] and the purity of mitochondria was checked by measuring activity of succinate dehydrogenase as described by King et al (1976).…”

Section: Preparation Of Subcellular Fractionsmentioning

confidence: 99%

4‐hydroxy tempo improves mitochondrial and neurobehavioral deficits in experimental model of Huntington's disease

Sandhir

Mahajan

Mehrotra

et al. 2015

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Mitochondrial dysfunctions have been implicated in the progression of Huntington's disease (HD). To date, several free radical scavengers have been tested in experimental HD, but only a few have shown promise. Although most antioxidants rapidly reduce ROS but in the process they are oxidized, which limits their ability to protect. Therefore, in the present study we employed a potent recycling antioxidant, 4-hydroxy tempo (4-HT), because it can reinstate its reduced state even after its oxidation during scavenging of ROS. Female Wistar rats were administered 3-nitropropionic acid (3-NP) and/or 4-HT for 21 days, after which animals were subjected to biochemical and behavioral assessments. Our results showed that 4-HT treatment significantly attenuated the 3-NP induced decrease in the activities of mitochondrial electron transport chain enzymes. In addition, 4-HT administration restored the increased nitrite and lipid peroxidation levels. Apart from this, 4-HT also attenuated the 3-NP induced decrease in superoxide dismutase and catalase activities. Further, 4-HT administration resulted in significant improvement in 3-NP induced cognitive and motor impairments. Taken together, the results of the study demonstrate that 4-HT is beneficial in 3-NP induced model of HD and thus could be a potential therapeutic agent in management of this disease.

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Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase

Cited by 46 publications

References 70 publications

The pro-oxidant chromium(VI) inhibits mitochondrial complex I, complex II, and aconitase in the bronchial epithelium: EPR markers for Fe–S proteins

The pro-oxidant chromium(VI) inhibits mitochondrial complex I, complex II, and aconitase in the bronchial epithelium: EPR markers for Fe–S proteins

Mitochondrial modulators in experimental Huntington’s disease: reversal of mitochondrial dysfunctions and cognitive deficits

4‐hydroxy tempo improves mitochondrial and neurobehavioral deficits in experimental model of Huntington's disease

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