Succinate dehydrogenase

Cerletti, Paolo; Giovenco, Maria Adelaide; Giordano, Maria; Giovenco, S.; Strom, Roberto

doi:10.1016/0005-2744(67)90223-9

Cited by 42 publications

(8 citation statements)

References 30 publications

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“…This was t o be expected, since the total phosphorus content of UQdepleted particles was almost the same (83O/,,) as before UQ extraction. It must be pointed out, on the other hand, that an effect of phospholipids could be demonstrated only when succinate dehydrogenase was solubilized in the presence of succinate [24], whereas reincorporation of UQ restored a higher succinate dehydrogenase activity to particles which had been depleted of UQ in the absence of succinate.…”

Section: Discussionmentioning

confidence: 95%

“…Cerletti et al [24] have shown that preincubation with phospholipids stimulates the activity of isolated succinate dehydrogenase, suggesting that the lipid environment is an important factor in regulating the catalytic properties of the enzyme. This conclusion was recently further supported by results obtained with phospholipase-treated mitochondria 1301.…”

Section: Discussionmentioning

confidence: 99%

“…Cerletti et al [24] have shown that the activity of isolated succinate dehydrogenase could be increased by preincubation of the enzyme with mitochondrial phospholipids. As shown in Fig.…”

Section: + Imentioning

confidence: 99%

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Studies with Ubiquinone‐Depleted Submitochondrial Particles

Rossi

Norling²,

Persson³

et al. 1970

European Journal of Biochemistry

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1. The effects of extraction and reincorporation of ubiquinone on the NADH and succinate dehydrogenase activities of submitochondrial particles from beef heart have been studied. 2.Extraction of ubiquinone had no effect on the maximal velocity or the K , for NADH of the NADH dehydrogenase of the particles measured with ferricyanide as electron acceptor.3. The succinate dehydrogenase activity of the particles, measured with phenazine methosulfate as electron acceptor, was diminished by approximately 50°/, upon the extraction of ubiquinone, and was restored when ubiquinone was reincorporated into the particles. Concomitantly, the K , for succinate decreased and increased upon the extraction and reincorporation of ubiquinone.4. Thenoyltrifluoroacetone, piericidin A, or pretreatment of the particles with cyanide, caused an approximately 50 decrease of the succinate dehydrogenase activity of the ubiquinonecontaining particles, while that of the ubiquinone-depleted particles was virtually unaffected by these agents.5. Addition of mitochondria1 phospholipids stimulated slightly the succinate dehydrogenase activity of both ubiquinone-containing and ubiquinone-depleted submitochondrial particles.6 . The data indicate that the succinate dehydrogenase of ubiquinone-depleted particles resembles in several respects preparations of isolated, soluble succinate dehydrogenase. It is concluded that the removal of ubiquinone causes a decrease in the rate of dissociation of fumarate from the enzyme and an inactivation ofthe interaction of its non-heme iron moiety with phenazine methosulfate. 7.It is pointed out that ubiquinone not only serves as an electron-transfer catalyst between succinate dehydrogenase and the cytochrome b-c, complex, but may also exert a regulatory effect on these entities.It has been reported [I] that extraction of ubiquinone from beef-heart submitochondrial particles ("EDTA particles") results in an inactivation of the NADH and succinate oxidase activities, which are restored by the reincorporation of ubiquinone into the particles. The site of inactivation was localized t o the electron-transfer step between the NADH and succinate dehydrogenase flavoproteins and cytochrome 6 , indicating that ubiquinone is an obligatory redox catalyst of the respiratory chain. I n the presence of antimycin A, cytochrome b was reduced by succinate (but not by NADH) in the ubiquinone-depleted particles, suggesting a modification of cytochrome b by antimycin A so as to interact with succinate dehydrogenase directly, without the mediation of ubi- quinone. Based on kinetic studies of the effect of antimycinA on the reduction of cytochrome b by succinate in ubiquinone-containing and ubiquinonedepleted particles, evidence was obtained [2] that ubiquinone, besides functioning as a redox catalyst, may exert a regulatory effect on the respiratory chain, being responsible for the sigmoidal kinetics of antimycin A inhibition of the cytochrome b -c, complex It was also found [4] that extraction of ubiquinone leads to a substantial decrea...

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

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Studies with Ubiquinone‐Depleted Submitochondrial Particles

Rossi

Norling²,

Persson³

et al. 1970

European Journal of Biochemistry

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“…The acidic phospholipids of cellular and intracellular membranes have been reported to be potential candidates for several functions: (a) activation [19], stabilization [20] and structural organization of the enzymes within the membranes [18], (b) the preferred site of association with cholesterol [21], (c) hormone responsiveness [22], (d) discrimination between permeability of univalent cations [23], (e) electrostatic interactions with proteins [24]. Although they are known to activate protein kinase C [25], the acidic phospholipids seem to act as inhibitors of some of the so-called soluble enzymes [6,9].…”

Section: Discussionmentioning

confidence: 99%

The influence of phosphatidate bilayers on pig heart AMP deaminase. Crucial role of pH-dependent lipid-phase transition

Woźniak

Kossowska

Purzycka-Preis

et al. 1988

Biochemical Journal

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Phosphatidate bilayers composed of dilauroylphosphatidate, dimyristoylphosphatidate, dipalmitoylphosphatidate and dioleoylphosphatidate were prepared. Their interaction with AMP deaminase isolated from pig heart was investigated. Dioleoylphosphatidate bilayers were found to exert non-competitive inhibition on the AMP deaminase with a K1 of 15 x 10-6 M. This inhibition is three orders of magnitude stronger than that exerted by orthophosphate. The phosphatidate species containing saturated fatty acids were either non-inhibitory or inhibited enzyme activity rather poorly. However, alkalinization of the medium from pH 6.5 to pH 7.9 led to the inhibition of pig heart AMP deaminase by dilauroylphosphatidate bilayers. This was accompanied by the fluidization of the saturated phosphatidate species, i.e. the lowering of their phase transition temperature in alkaline pH, as measured by light-scattering and fluorescence scans. The possible significance of these findings for the regulation of AMP deaminase activity in vivo by natural membranes is discussed.

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“…Cerletti et al (109,111) reported that the activity of purified preparations of the dehydrogenase is stimulated by certain phospholipids. Under the same conditions lipids had no effect on the activity in mitochondria.…”

Section: A Factors Affecting Activity Measurementsmentioning

confidence: 99%