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PubMed1997

The carboxyl terminus of the Saccharomyces cerevisiae succinate dehydrogenase membrane subunit, SDH4p, is necessary for ubiquinone reduction and enzyme stability.

The succinate dehydrogenase (SDH) of Saccharomyces cerevisiae is composed of four nonidentical subunits encoded by the nuclear genes SDH1, SDH2, SDH3, and SDH4. The hydrophilic subunits, SDH1p and SDH2p, comprise the catalytic domain involved in succinate oxidation. They are anchored to the inner mitochondrial membrane by two small, hydrophobic subunits, SDH3p and SDH4p, which are required for electron transfer and ubiquinone reduction. Comparison of the deduced primary sequence of the yeast SDH4p subunit to SDH4p subunits from other species reveals the presence of an unusual 25-30 amino acid carboxyl-terminal extension following the last predicted transmembrane domain. The extension is predicted to be on the cytoplasmic side of the inner mitochondrial membrane. To investigate the extension's function, three truncations were created and characterized. The results reveal that the carboxyl-terminal extension is necessary for respiration and growth on nonfermentable carbon sources, for ubiquinone reduction, and for enzyme stability. Combined with inhibitor studies using a ubiquinone analog, our results suggest that the extension and more specifically, residues 128-135 are involved in the formation of a ubiquinone binding site. Our findings support a two-ubiquinone binding site model for the S. cerevisiae SDH.

2,4-Dinitrophenol↗
PubMed1999

Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase.

The smallest membrane-anchoring subunit (QPs3) of bovine heart succinate:ubiquinone reductase was overexpressed in Escherichia coli JM109 as a glutathione S-transferase fusion protein using the expression vector pGEX2T/QPs3. The yield of soluble active recombinant glutathione S-transferase-QPs3 fusion protein was isopropyl-1-thio-beta-D-galactopyranoside concentration-, induction growth time-, temperature-, and medium-dependent. Maximum yield of soluble recombinant fusion protein was obtained from cells harvested 3.5 h post-isopropyl-1-thio-beta-D-galactopyranoside (0.4 mM)-induction growth at 25 degrees C in 2.0% tryptone, 0.5% yeast extract, 10 mM NaCl, 2.5 mM KCl, 10 mM MgCl2, 20 mM glucose (SOC medium) containing 440 mM sorbitol and 2.5 mM betaine. QPs3 was released from the fusion protein by proteolytic cleavage with thrombin. Isolated recombinant QPs3 shows one protein band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis that corresponds to subunit V of mitochondrial succinate:ubiquinone reductase. Although purified recombinant QPs3 is dispersed in 0.01% dodecylmaltoside, it is in a highly aggregated form, with an apparent molecular mass of more than 1 million. The recombinant QPs3 binds ubiquinone, causing a spectral blue shift. Upon titration of the recombinant protein with ubiquinone, a saturation behavior is observed, suggesting that the binding is specific and that recombinant QPs3 may be in the functionally active state. Two amino acid residues, serine 33 and tyrosine 37, in the putative ubiquinone binding domain of QPs3 are involved in ubiquinone binding because the S33A- or Y37A-substituted recombinant QPs3s do not cause the spectral blue shift of ubiquinone. Although recombinant QPs3 contains little cytochrome b560 heme, the spectral characteristics of cytochrome b560 are reconstituted upon addition of hemin chloride. Reconstituted cytochrome b560 in recombinant QPs3 shows a EPR signal at g = 2.92. Histidine residues at positions 46 and 60 are responsible for heme ligation because the H46N- or H60N-substituted QPs3 fail to restore cytochrome b560 upon addition of hemin chloride.

Animals↗
PubMed1999

The Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase. Identification of Sdh3p amino acid residues involved in ubiquinone binding.

Succinate dehydrogenase (SDH) participates in the mitochondrial electron transport chain by oxidizing succinate to fumarate and transferring the electrons to ubiquinone. In yeast, it is composed of a catalytic dimer, comprising the Sdh1p and Sdh2p subunits, and a membrane domain, comprising two smaller hydrophobic subunits, Sdh3p and Sdh4p, which anchor the enzyme to the mitochondrial inner membrane. To investigate the role of the Sdh3p anchor polypeptide in enzyme assembly and catalysis, we isolated and characterized seven mutations in the SDH3 gene. Two mutations are premature truncations of Sdh3p with losses of one or three transmembrane segments. The remaining five are missense mutations that are clustered between amino acids 103 and 117, which are proposed to be located in transmembrane segment II or the matrix-localized loop connecting segments II and III. Three mutations, F103V, H113Q, and W116R, strongly but specifically impair quinone reductase activities but have only minor effects on enzyme assembly. The clustering of the mutations strongly suggests that a ubiquinone-binding site is associated with this region of Sdh3p. In addition, the biphasic inhibition of quinone reductase activity by a dinitrophenol inhibitor supports the hypothesis that two distinct quinone-binding sites are present in the yeast SDH.

Amino Acid Sequence↗
PubMed2001

Retention of heme in axial ligand mutants of succinate-ubiquinone xxidoreductase (complex II) from Escherichia coli.

Succinate-ubiquinone oxidoreductase (SdhCDAB, complex II) from Escherichia coli is a four-subunit membrane-bound respiratory complex that catalyzes ubiquinone reduction by succinate. In the E. coli enzyme, heme b(556) is ligated between SdhC His(84) and SdhD His(71). Contrary to a previous report (Vibat, C. R. T., Cecchini, G., Nakamura, K., Kita, K., and Gennis, R. B. (1998) Biochemistry 37, 4148-4159), we demonstrate the presence of heme in both SdhC H84L and SdhD H71Q mutants of SdhCDAB. EPR spectroscopy reveals the presence of low spin heme in the SdhC H84L (g(z) = 2.92) mutant and high spin heme in the SdhD H71Q mutant (g = 6.0). The presence of low spin heme in the SdhC H84L mutant suggests that the heme b(556) is able to pick up another ligand from the protein. CO binds to the reduced form of the mutants, indicating that it is able to displace one of the ligands to the low spin heme of the SdhC H84L mutant. The g = 2.92 signal of the SdhC H84L mutant titrates with a redox potential at pH 7.0 (E(m)(,7)) of approximately +15 mV, whereas the g = 6.0 signal of the SdhD H71Q mutant titrates with an E(m)(,7) of approximately -100 mV. The quinone site inhibitor pentachlorophenol perturbs the heme optical spectrum of the wild-type and SdhD H71Q mutant enzymes but not the SdhC H84L mutant. This finding suggests that the latter residue also plays an important role in defining the quinone binding site of the enzyme. The SdhC H84L mutation also results in a significant increase in the K(m) and a decrease in the k(cat) for ubiquinone-1, whereas the SdhD H71Q mutant has little effect on these parameters. Overall, these data indicate that SdhC His(84) has an important role in defining the interaction of SdhCDAB with both quinones and heme b(556).

Benzoquinones↗
PubMed2001

Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase.

IMP-1 metallo-beta-lactamase (class B) is a plasmid-borne zinc metalloenzyme that efficiently hydrolyzes beta-lactam antibiotics, including carbapenems, rendering them ineffective. Because IMP-1 has been found in several clinically important carbapenem-resistant pathogens, there is a need for inhibitors of this enzyme that could protect broad spectrum antibiotics such as imipenem from hydrolysis and thus extend their utility. We have identified a series of 2,3-(S,S)-disubstituted succinic acids that are potent inhibitors of IMP-1. Determination of high resolution crystal structures and molecular modeling of succinic acid inhibitor complexes with IMP-1 has allowed an understanding of the potency, stereochemistry, and structure-activity relationships of these inhibitors.

Crystallography, X-Ray↗
PubMed2002

Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase.

Oxidative stress is created in aerobic organisms when molecular oxygen chemically oxidizes redox enzymes, forming superoxide (O2*-) and hydrogen peroxide (H2O2). Prior work identified several flavoenzymes from Escherichia coli that tend to autoxidize. Of these, fumarate reductase (Frd) is notable both for its high turnover number and for its production of substantial O2*- in addition to H2O2. We have sought to identify characteristics of Frd that predispose it to this behavior. The ability of excess succinate to block autoxidation and the inhibitory effect of lowering the flavin potential indicate that all detectable autoxidation occurs from its FAD site, rather than from iron-sulfur clusters or bound quinones. The flavin adenine dinucleotide (FAD) moiety of Frd is unusually solvent-exposed, as evidenced by its ability to bind sulfite, and this may make it more likely to react adventitiously with O2*-. The autoxidizing species is apparently fully reduced flavin rather than flavosemiquinone, since treatments that more fully reduce the enzyme do not slow its turnover number. They do, however, switch the major product from O2*- to H2O2. A similar effect is achieved by lowering the potential of the proximal [2Fe-2S] cluster. These data suggest that Frd releases O2*- into bulk solution if this cluster is available to sequester the semiquinone electron; otherwise, that electron is rapidly transferred to the nascent superoxide, and H2O2 is the product that leaves the active site. This model is supported by the behavior of "aspartate oxidase" (aspartate:fumarate oxidoreductase), an Frd homologue that lacks Fe-S clusters. Its dihydroflavin also reacts avidly with oxygen, and H2O2 is the predominant product. In contrast, succinate dehydrogenase, with high potential clusters, generates O2*- exclusively. The identities of enzyme autoxidation products are significant because O2*- and H2O2 damage cells in different ways.

Amino Acid Oxidoreductases↗
PubMed2005

Electron transfer within complex II. Succinate:ubiquinone oxidoreductase of Escherichia coli.

Electron transfer within Escherichia coli succinate:ubiquinone oxidoreductase has been examined by the pulse radiolysis technique using spectrophotometric detection. Electrons have been introduced into the protein by the bimolecular reaction with quantified concentrations of the low potential N-methylnicotinamide radical at a rate constant of 7 x 10(8) M(-1) s(-1). Two redox-active centers in the protein are initially reduced, assigned as the high potential [3Fe-4S] center and the bound ubiquinone, followed by intramolecular equilibration with the b heme in both cases. Electron equilibration at 25 degrees C from the ubisemiquinone proceeds with an observed rate constant of 7,200 s(-1) and from the more distant [3Fe-4S] reduced center at a rate constant of 1,200 s(-1). Temperature dependence studies have revealed that both reactions have large free energies of activation, with deltaG(double dagger) values of +0.53 and +0.58 eV, respectively. Cumulative spectral changes, as well as accompanying decreases in the rates of intramolecular electron transfer, observed upon adding electrons to progressively reduced protein, indicate that 4 electrons must be introduced into the protein before the heme center is fully reduced. Overall, evidence is presented that the heme, far from being a bystander in the efficient transfer of reducing equivalents from succinate to the ubiquinone via the flavin-Fe/S centers, plays a pivotal role in providing a lower energy pathway for the transfer of an electron from the high potential [3Fe-4S] center to ubiquinone.

Coenzymes↗
PubMed1975

Affinity chromatography of succinate dehydrogenase from the membranes of Micrococcus lysodeikticus.

Isolated plasma membranes of Micrococcus lysodeikticus were subjected to extraction with n-butanol in a two-phase system. Succinate dehydrogenase obtained in the soluble aqueous phase after high-speed centrifugation was resolved by separation on calcium phosphate gel and affinity chromatography. The affinity ligand used was oxaloacetate and elution from the column was achieved with 0.5 M succinate. In the final product there was an eleven-fold reduction in the 32P-lipid to protein ratio and a fourteen-fold increase in specific activity relative to the high speed supernatant fraction following n-butanol extraction.

Cell Membrane↗
PubMed1955

The distribution of histochemically demonstrable succinic dehydrogenase and of mitochondria in tongue and skeletal muscles.

Various skeletal muscles show considerable variations in histochemically demonstrable succinic dehydrogenase activity. In muscles from the lower extremities, the back, and the abdominal wall, only some fibers reveal evidence of enzymatic staining. In the diaphragm and masseter more fibers react positively. In the tongue, however, all fibers show marked activity comparable to that found regularly in the heart. There is a close similarity in the distribution of histochemically demonstrable succinic dehydrogenase and stainable mitochondria in tissue sections.

Mitochondria↗
PubMed1976

Effect of dilauryl succinate on reproduction of the cock and hen and preventive effect of vitamin E.

Fertility of White Leghorn cocks fed a diet containing 12% of dilauryl succinate (LS) for 16 weeks was significantly lower than that of cocks fed the control diet. Little difference in fertility and hatchability of fertile eggs was observed between White Leghorn hens fed the control or LS diets, but the percentage of chicks at hatch, which showed signs of encephalomalacia with lesions on the cerebellum, and the percentage of the hens and offspring having fragile erythrocytes were much higher when LS was fed. Total tocopherol in the plasma of the cocks and hens fed LS and in the eggs laid by the hens fed LS was lower than that in birds fed the control diet, though that of the hens was within the range of plasma tocopherol of normal hens. Offspring of the cocks and hens fed LS died from encephalomalacia earlier than those fed the control diet. These observations with LS feeding were all prevented by oral administration of dl-alpha-tocopheryl acetate. The responses of the cocks and hens to LS were compared with those to linoleic acid in the literature. The direct effect of LS, or more likely of monolauryl succinate, independent of peroxides from unsaturated fatty acids was discussed.

Animals↗
PubMed1998

Improved viability and metabolic behavior of hepatocytes after liver storage in the presence of a succinic acid ester.

BACKGROUND: Selected esters of succinic acid were recently proposed as novel nutrients to support ATP generation in cells endangered by an imbalance between the formation and breakdown of this adenine nucleotide. In the present study, a new ester, glycerol-1,2,3-trimethylsuccinate, was examined for its potential beneficial effect in the procedures preceding liver transplantation. METHODS: The viability and metabolic behavior of hepatocytes were examined after perfusion and storage of rat livers for 20 hr at 4 degrees C with a Belzer UW-CSS solution in the absence or presence or 2 mM glycerol-1,2,3-trimethylsuccinate. RESULTS: Although it failed to affect significantly the release of cellular enzymes during storage and the protein or glycogen content of the liver, and was unable to prevent the storage-induced decrease in both biosynthetic activity and D-[U-14C]glucose incorporation into glycogen in isolated hepatocytes, the ester restored to a close-to-normal value the viability of the hepatocytes and opposed the starvation-like effects of liver storage upon both the conversion of D-[U-14C]glucose to 14CO2 and radioactive amino acids and the de novo generation of 14C-labeled D-glucose from [2-14C]pyruvate. CONCLUSIONS: Because succinic acid esters are efficiently metabolized in several cell types, the present results suggest that such esters may have a wide field of application in transplantation procedures.

Animals↗
PubMed1995

Succiniclasticum ruminis gen. nov., sp. nov., a ruminal bacterium converting succinate to propionate as the sole energy-yielding mechanism.

A gram-negative, anaerobic, nonmotile, non-spore-forming, rod-shaped bacterium that fermented succinate quantitatively to propionate was isolated from a high dilution of rumen ingesta obtained from a dairy cow fed a production diet containing grass silage as the main roughage source. This organism did not grow on any of the following energy sources: 12 carbohydrates, pyruvate, lactate, 7 dicarboxylic acids, aspartate, citrate, and trans-aconitate. Both rumen fluid and yeast extract were necessary for good growth on succinate. The organism was negative for the following characteristics: production of propionate from threonine, protein digestion, sulfide production, nitrate reduction, catalase activity, and urease activity. There was no growth at 22 degrees C and reduced growth at 45 degrees C compared with growth at 39 degrees C. The DNA base composition was 52 mol% G + C. The complete 16S rRNA sequence (EMBL accession number, X81137) was obtained, and the phylogenetic relationships of the organism were determined. The most closely related genera were the genera Acidaminococcus and Phascolarctobacterium. The name proposed for this bacterium is Succiniclasticum ruminis gen. nov., sp. nov.; the type strain is strain SE10 (= DSM 9236). Additional isolation attempts revealed that S. ruminis is a common inhabitant of the rumina of cows that are fed production diets and of cows on pasture.

Animals↗
PubMed1982

Effects of anaerobiosis and nitrate on the expression of succinate dehydrogenase and enzymes associated with nitrogen metabolism in Klebsiella pneumoniae.

We have shown that the low histidase activity found in anaerobic, nitrogen-limited cultures of Klebsiella pneumoniae is due to repression of the right-hand hut operon. In addition, we have examined the effects of NO3- on the aerobic and anaerobic expression of catabolite- and NH4+-repressible enzymes in this organism. NO3- permitted anaerobic growth of K. pneumoniae in minimal medium containing histidine as the sole carbon source, and histidase and succinate dehydrogenase were derepressed during anaerobic growth in histidine/NO3- medium. Use of sucrose rather than histidine as the carbon source reversed the effects of NO3- and repressed histidase and succinate dehydrogenase activities. Anaerobic growth in sucrose/NO3- medium also uncoupled the expression of urease and glutamine synthetase.

Anaerobiosis↗
PubMed1999

Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides.

Succinic semialdehyde dehydrogenase (SSADH) is one of three enzymes constituting the gamma-aminobutyric acid shunt. We have cloned the cDNA for SSADH from Arabidopsis, which we designated SSADH1. SSADH1 cDNA encodes a protein of 528 amino acids (56 kD) with high similarity to SSADH from Escherichia coli and human (>59% identity). A sequence similar to a mitochondrial protease cleavage site is present 33 amino acids from the N terminus, indicating that the mature mitochondrial protein may contain 495 amino acids (53 kD). The native recombinant enzyme and the plant mitochondrial protein have a tetrameric molecular mass of 197 kD. Fractionation of plant mitochondria revealed its localization in the matrix. The purified recombinant enzyme showed maximal activity at pH 9.0 to 9.5, was specific for succinic semialdehyde (K(0.5) = 15 microM), and exclusively used NAD+ as a cofactor (Km = 130 +/- 77 microM). NADH was a competitive inhibitor with respect to NAD+ (Ki = 122 +/- 86 microM). AMP, ADP, and ATP inhibited the activity of SSADH (Ki = 2.5-8 mM). The mechanism of inhibition was competitive for AMP, noncompetitive for ATP, and mixed competitive for ADP with respect to NAD+. Plant SSADH may be responsive to mitochondrial energy charge and reducing potential in controlling metabolism of gamma-aminobutyric acid.

Adenine Nucleotides↗
PubMed1969

The respiratory chain of plant mitochondria. I. Electron transport between succinate and oxygen in skunk cabbage mitochondria.

The kinetics of oxidation of ubiquinone, flavoprotein, cytochrome c, and the cytochrome b complex in skunk cabbage (Symplocarpus foetidus) mitochondria made anaerobic with succinate have been measured spectrophotometrically and fluorimetrically in the absence of respiratory inhibitor and in the presence of cyanide or antimycin A. No component identifiable by these means was oxidized rapidly enough in the presence of one or the other inhibitor to qualify for the role of alternate oxidase. Cycles of oxidation and rereduction of flavoprotein and ubiquinone obtained by injecting 12 mum oxygen into the anaerobic mitochondrial suspension were kinetically indistinguishable in the presence of cyanide or antimycin A, implying that these 2 components are part of a respiratory pathway between succinate and oxygen which does not involve the cytochromes and does involve a cyanide-insensitive alternate oxidase. The cytochrome b complex shows biphasic oxidation kinetics with half times of 0.018 sec and 0.4 sec in the absence of inhibitor, which increase to 0.2 sec and 1 sec in the presence of cyanide. In the presence of antimycin A, the oxidation of the cytochrome b complex shows an induction period of 1 sec and a half-time of 3.5 sec. A split respiratory chain with 2 terminal oxidases and a branch point between the cytochromes and flavoprotein and ubiquinone is proposed for these mitochondria.

Electron Transport↗
PubMed1969

The effect of respiratory inhibitors on NADH, succinate and malate oxidation in corn mitochondria.

The effect of a series of respiratory inhibitors on the oxidation of NADH in state 4 and state 3 conditions was studied with corn shoot mitochondria. Comparisons were made using malate and succinate as substrates. The inhibitors, rotenone, amytal, antimycin A and cyanide, inhibited oxidation of NADH in state 3 but rotenone and amytal did not inhibit oxidation in state 4. The inhibition by antimycin A was partially overcome by the presence of cytochrome c. The results indicate the presence of alternative pathways available for NADH oxidation depending on the metabolic condition of the mitochondria. Under state 4 conditions, NADH oxidation bypasses the amytal and rotenone sensitive sites but under state 3 conditions a component of the NADH respiration appears to be oxidized by an internal pathway which is sensitive to these inhibitors. Still a third pathway for NADH oxidation is dependent on the addition of cytochrome c and is insensitive to antimycin A. Succinate oxidation was sensitive to cyanide and antimycin A under both state 4 and state 3 conditions as well as amytal and rotenone under state 3 conditions but was not inhibited by amytal and rotenone under state 4 conditions. Malate oxidation was inhibited by cyanide, rotenone and amytal under both state 4 and state 3 conditions. Antimycin A inhibited state 3 but did not appreciably alter state 4 rates of malate oxidation. With all substrates tested inhibition by antimycin A was greatly facilitated by preswelling the mitochondria for 10 min. This was interpreted to indicate that swelling increases the accessibility of antimycin A to the site of inhibition.

Amobarbital↗
PubMed1986

Mechanisms of triple stress-mediated damage in stationary phase cells of Salmonella typhimurium exposed to succinate-acidified hypochlorite system at 5 degrees C.

Exposure for 20 min of stationary phase cells of Salmonella typhimurium to a combined triple stress system (TSS) treatment comprising hypochlorite derived 5 ppm free available chlorine in solution acidified with 1% succinate (pH 2.5) and at a chill shock temperature of 5 degrees C resulted in symptoms of injury. Cells became sensitive to 40 micrograms/ml lysozyme, 50 micrograms/ml actinomycin D and 100 micrograms/ml ribonuclease B, to which control cells were resistant. Metabolic injury was indicated by reduction in colony forming ability of stressed cells on minimal salts glucose agar M9 medium. There was no detectable leakage loss of 260-280 nm-absorbing materials. This was also confirmed by assay of the cellular RNA material components. Loss of alkaline phosphatase activity was observed in the stressed cells. The intensity of induced cellular damage as measured by lysozyme sensitivity was greatest in the cells exposed to the complete TSS, followed by those stressed in 1% succinate at 5 degrees C, then 5 ppm chlorine at 5 degrees C and the singular chill shock stress at 5 degrees C, respectively. The magnitudes of cellular damage, however, were suggestive of synergistic interactions among the component stress factors of the TSS. The findings obtained indicated impairment of the structural integrity and functional capabilities of the permeability barriers and the inactivation of certain periplasmic enzymes. The resultant cumulative cellular damage from the TSS exposure may therefore enhance greater sensitivity of treated cells to subsequent stress factors.

Alkaline Phosphatase↗
PubMed2005

Enhancement of lactate and succinate formation in adhE or pta-ackA mutants of NADH dehydrogenase-deficient Escherichia coli.

AIMS: The aim of the study is to investigate the effect of multiple mutations in redox or energy producing pathways of Escherichia coli on metabolic product distribution in anaerobic-rich media cultures. METHODS AND RESULTS: Various combinations of NADH dehydrogenase (NDH)-deficient, alcohol dehydrogenase (ADH), and phosphotransacetylase and acetate kinase (PTA-ACK) mutants were constructed. Anaerobic LB-glucose cultures of the strains were grown and extracellular metabolites were analysed and compared with those of the parental strain, E. coli MG1655. The profile of metabolites was examined in log phase and 24-h cultures. CONCLUSIONS: Inactivation of ndh and/or nuo gene leads to higher production of d-lactate, ethanol, formate and succinate in log phase. Inactivation of pta-ackA in NDH-I- or NDH-II-deficient strains lead to increased D-lactate formation and decreased ethanol formation. Removal of ethanol production by adhE gene inactivation generated higher production of succinate and D-lactate. D-lactate was the primary product in the ndh nuo adhE strain. SIGNIFICANCE AND IMPACT OF THE STUDY: The results show the effects of altering NADH utilization pathways on distribution of metabolic products. Such information improves our understanding of metabolic shifts and may find application in metabolic engineering of E. coli.

Alcohol Dehydrogenase↗