Gene Symbol: sdhA
Description: succinate dehydrogenase, flavoprotein subunit
Alias: ECK0712, JW0713
Species: Escherichia coli str. K-12 substr. MG1655
Products:     sdhA

Top Publications

  1. Iuchi S, Aristarkhov A, Dong J, Taylor J, Lin E. Effects of nitrate respiration on expression of the Arc-controlled operons encoding succinate dehydrogenase and flavin-linked L-lactate dehydrogenase. J Bacteriol. 1994;176:1695-701 pubmed
    ..g., cyoABCDE (encoding the cytochrome o complex), cydAB (encoding the cytochrome d complex), and sodA (encoding the manganese-dependent superoxide dismutase). ..
  2. Takeda S, Matsushika A, Mizuno T. Repression of the gene encoding succinate dehydrogenase in response to glucose is mediated by the EIICB(Glc) protein in Escherichia coli. J Biochem. 1999;126:354-60 pubmed
    ..These results support the view that the EIICB(Glc) protein functions not only as a glucose transporter, but also as a glucose-sensing signal transducer that modulates the glucose repression of the sdhCDAB operon. ..
  3. Mass E, Gottesman S. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci U S A. 2002;99:4620-5 pubmed publisher
  4. Wilde R, Guest J. Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12. J Gen Microbiol. 1986;132:3239-51 pubmed
    ..Sequences resembling known binding sites for the cAMP-CRP (cyclic AMP-cyclicAMP receptor protein) complex occur in the vicinity of each promoter suggesting that they are activated by the cAMP-CRP complex. ..
  5. Park S, Tseng C, Gunsalus R. Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr. Mol Microbiol. 1995;15:473-82 pubmed
    ..Iron and haem availability affected sdhC-lacZ expression by two- to three-fold. Lastly, sdhC-lacZ expression was shown to vary with the cell growth rate during aerobic and anaerobic conditions. ..
  6. Cecchini G, Schröder I, Gunsalus R, Maklashina E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim Biophys Acta. 2002;1553:140-57 pubmed
    ..The structure and function of SQR and QFR are briefly summarized in this communication and the similarities and differences in the membrane domain of the two enzymes are discussed. ..
  7. Shen J, Gunsalus R. Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB) gene expression in Escherichia coli. Mol Microbiol. 1997;26:223-36 pubmed
    ..Lastly, the Fnr-dependent control of sdhCDAB gene expression was shown to occur independently of the ArcA and to require DNA sequences near the start of sdhC transcription. ..
  8. Tomasiak T, Maklashina E, Cecchini G, Iverson T. A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II. J Biol Chem. 2008;283:15460-8 pubmed publisher
    ..Taken together, hydrogen bonding from act-T to substrate may coordinate with interdomain motions to twist the double bond of fumarate and introduce the strain important for attaining the transition state. ..
  9. Cheng V, Ma E, Zhao Z, Rothery R, Weiner J. The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow. J Biol Chem. 2006;281:27662-8 pubmed
    ..We hypothesize that this occurs because the midpoint potentials of the [Fe-S] clusters in the native enzyme are poised such that direction of electron transfer from succinate to ubiquinone is favored. ..

More Information


  1. Ackrell B. Progress in understanding structure-function relationships in respiratory chain complex II. FEBS Lett. 2000;466:1-5 pubmed
    ..These offer new insights into structure-function relationships of this class of flavoenzymes, including evidence favoring protein movement during catalysis...
  2. Iuchi S, Cameron D, Lin E. A second global regulator gene (arcB) mediating repression of enzymes in aerobic pathways of Escherichia coli. J Bacteriol. 1989;171:868-73 pubmed
    ..The arcB product might be a sensor protein for the redox or energy state of the arc regulatory system. ..
  3. Zhdan Pushkina S, Verbitskaia N, Kondrat eva L. [Succinate dehydrogenase activity of Escherichia coli cells after heat stress and during the reparative process]. Mikrobiologiia. 1986;55:357-61 pubmed
    ..The SDH activity of the cell-free extracts did not change after their heating at 48 degrees C. The SDH activity of E. coli cells is recommended to be used as a parameter indicative of their stress state. ..
  4. Wrightstone R, Smith L, Wilson J, Vella F, Huisman T. Some physicochemical properties of hemoglobin-manitoba (alpha2 102Ser replaced by Arg (G9) beta2). Biochim Biophys Acta. 1975;412:283-7 pubmed
  5. Barker H, Kinsella N, Jaspe A, Friedrich T, O Connor C. Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide. Mol Microbiol. 2000;35:1518-29 pubmed
    ..Additionally, protective quantities of formate are secreted by E. coli and Salmonella during growth suggesting that such compounds are important determinants of bacterial survival in the host. ..
  6. Yang X, Yu L, Yu C. Resolution and reconstitution of succinate-ubiquinone reductase from Escherichia coli. J Biol Chem. 1997;272:9683-9 pubmed
  7. Magnusson K, Philips M, Guest J, Rutberg L. Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex. J Bacteriol. 1986;166:1067-71 pubmed
    ..An open reading frame corresponding to the structural gene, sdhA, for cytochrome b558 was identified...
  8. Wood D, Darlison M, Wilde R, Guest J. Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Biochem J. 1984;222:519-34 pubmed
    The nucleotide sequence of a 3614 base-pair segment of DNA containing the sdhA gene, encoding the flavoprotein subunit of succinate dehydrogenase of Escherichia coli, and two genes sdhC and sdhD, encoding small hydrophobic subunits, has ..
  9. Zhao Z, Rothery R, Weiner J. Effects of site-directed mutations in Escherichia coli succinate dehydrogenase on the enzyme activity and production of superoxide radicals. Biochem Cell Biol. 2006;84:1013-21 pubmed
    ..1 to 10 mmol/L. Our results indicate that, in SdhCDAB, the Q site with bound ubiquinone is an important source of superoxide radicals. ..
  10. Cheng V, Johnson A, Rothery R, Weiner J. Alternative sites for proton entry from the cytoplasm to the quinone binding site in Escherichia coli succinate dehydrogenase. Biochemistry. 2008;47:9107-16 pubmed publisher
    ..On the basis of these results we propose an alternative proton pathway in E. coli Sdh that might be functional only in vitro. ..
  11. Messner K, Imlay J. Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. J Biol Chem. 2002;277:42563-71 pubmed
    ..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. ..
  12. Fischer E, Sauer U. A novel metabolic cycle catalyzes glucose oxidation and anaplerosis in hungry Escherichia coli. J Biol Chem. 2003;278:46446-51 pubmed
  13. Vibat C, Cecchini G, Nakamura K, Kita K, Gennis R. Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli. Biochemistry. 1998;37:4148-59 pubmed
    ..the subunits (SDHC and SDHD) are hydrophobic and anchor the two more hydrophilic (flavin and iron-sulfur) subunits (SDHA and SDHB) to the cytoplasmic membrane...
  14. Yang X, Yu L, He D, Yu C. The quinone-binding site in succinate-ubiquinone reductase from Escherichia coli. Quinone-binding domain and amino acid residues involved in quinone binding. J Biol Chem. 1998;273:31916-23 pubmed
    ..The hydroxyl group, but not the size of the amino acid side chain, at position 33 of SdhC is also important, because Ser-33 can be substituted with threonine but not with alanine. ..
  15. Swim H, Krampitz L. Acetic acid oxidation by Escherichia coli; evidence for the occurrence of a tricarboxylic acid cycle. J Bacteriol. 1954;67:419-25 pubmed
  16. Calhoun M, Newton G, Gennis R. E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli. J Bacteriol. 1991;173:1569-70 pubmed
  17. Condon C, Cammack R, Patil D, Owen P. The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex. J Biol Chem. 1985;260:9427-34 pubmed
    ..Midpoint redox potentials of Centers 1-3 for both the membrane-bound and detergent-solubilized enzyme were estimated to be +10 mV, -175 mV, and +65 mV, respectively. ..
  18. Shimizu H, Nihei C, Inaoka D, Mogi T, Kita K, Harada S. Screening of detergents for solubilization, purification and crystallization of membrane proteins: a case study on succinate:ubiquinone oxidoreductase from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008;64:858-62 pubmed publisher
    ..Crystallization took place before detergent phase separation occurred and the type of detergent mixture affected the crystal form. ..
  19. Nam T, Park Y, Jeong H, Ryu S, Seok Y. Glucose repression of the Escherichia coli sdhCDAB operon, revisited: regulation by the CRP*cAMP complex. Nucleic Acids Res. 2005;33:6712-22 pubmed
    ..cAMP level in the presence of glucose is the major determinant of the glucose repression of the sdhCDAB operon. ..
  20. Matsushika A, Mizuno T. A dual-signaling mechanism mediated by the ArcB hybrid sensor kinase containing the histidine-containing phosphotransfer domain in Escherichia coli. J Bacteriol. 1998;180:3973-7 pubmed
    ..Based on these and other in vivo results, we propose a model in which ArcB functions in its own right as a dual-signaling sensor that is capable of propagating two types of stimuli through two distinct phosphotransfer pathways. ..
  21. Guest J. Partial replacement of succinate dehydrogenase function by phage- and plasmid-specified fumarate reductase in Escherichia coli. J Gen Microbiol. 1981;122:171-9 pubmed
  22. Tran Q, Rothery R, Maklashina E, Cecchini G, Weiner J. The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b. J Biol Chem. 2006;281:32310-7 pubmed
    ..Overall, these results demonstrate the importance of a functional, semiquinone-stabilizing Q(P) site for the observation of rapid succinate-dependent heme reduction. ..
  23. Maklashina E, Cecchini G. Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli. Arch Biochem Biophys. 1999;369:223-32 pubmed
    ..The pH activity profiles for E. coli QFR and SQR are similar showing maximal activity between pH 7.4 and 7.8, suggesting the importance of similar catalytic groups in quinol deprotonation and oxidation. ..
  24. Mewies M, McIntire W, Scrutton N. Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current state of affairs. Protein Sci. 1998;7:7-20 pubmed
    ..Case studies are presented for a variety of covalent flavoenzymes, from which general findings are beginning to emerge. ..
  25. Kita K, Vibat C, Meinhardt S, Guest J, Gennis R. One-step purification from Escherichia coli of complex II (succinate: ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556. J Biol Chem. 1989;264:2672-7 pubmed
    ..The enzyme has been reconstituted in phospholipid vesicles and demonstrated to reduce ubiquinone-8, the natural electron acceptor, at a high rate. ..
  26. Oden K, DeVeaux L, Vibat C, Cronan J, Gennis R. Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA. Gene. 1990;96:29-36 pubmed
    ..It is reported that such mutants may be constructed without linearizing plasmid DNA, as described previously. ..
  27. Lin H, Bennett G, San K. Genetic reconstruction of the aerobic central metabolism in Escherichia coli for the absolute aerobic production of succinate. Biotechnol Bioeng. 2005;89:148-56 pubmed
    ..Nevertheless, this aerobic succinate production system provides the first platform for enhancing succinate production aerobically in E. coli based on the creation of a new aerobic central metabolic network. ..
  28. Maklashina E, Rothery R, Weiner J, Cecchini G. Retention of heme in axial ligand mutants of succinate-ubiquinone xxidoreductase (complex II) from Escherichia coli. J Biol Chem. 2001;276:18968-76 pubmed
    ..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). ..
  29. Maklashina E, Cecchini G. The quinone-binding and catalytic site of complex II. Biochim Biophys Acta. 2010;1797:1877-82 pubmed publisher
    ..These data suggest that movement of the quinone within the quinone-binding pocket is essential for catalysis. ..
  30. Kita K, Yamato I, Anraku Y. Purification and properties of cytochrome b556 in the respiratory chain of aerobically grown Escherichia coli K12. J Biol Chem. 1978;253:8910-5 pubmed
    ..The molar extinction coefficient of cytochrome b556 was determined as 22.8 cm-1 mM-1. Its oxidation-reduction potential was found to be -45 mV. It could be reduced by D-lactate dehydrogenase of E. coli in the presence of menadione. ..
  31. Nakamura K, Yamaki M, Sarada M, Nakayama S, Vibat C, Gennis R, et al. Two hydrophobic subunits are essential for the heme b ligation and functional assembly of complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli. J Biol Chem. 1996;271:521-7 pubmed
    ..coli complex II in the membrane. Accumulation of the catalytic portion in the cytoplasm was found when sdhCDAB was introduced into a heme synthesis mutant, suggesting the importance of heme in the assembly of E. coli complex II. ..
  32. Mattevi A, Tedeschi G, Bacchella L, Coda A, Negri A, Ronchi S. Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Structure. 1999;7:745-56 pubmed
    ..Thus, LASPO, SDH and FRD form a class of functionally and structurally related oxidoreductases that are all able to reduce fumarate and to oxidise a dicarboxylate substrate. ..
  33. Ruprecht J, Yankovskaya V, Maklashina E, Iwata S, Cecchini G. Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site. J Biol Chem. 2009;284:29836-46 pubmed publisher
  34. Gao S, Zhang W, Wang J, Guo A. [Integration and expression of sdh gene in Escherichia coli]. Wei Sheng Wu Xue Bao. 2005;45:139-41 pubmed
    ..The PCR products assay using the upstream and downstream sequences of ptsG gene as primers and JM109s genomic DNA as template, indicated that sdh gene had been integrated at the ptsG gene site in Escherichia coli. ..
  35. Hagerhall C. Succinate: quinone oxidoreductases. Variations on a conserved theme. Biochim Biophys Acta. 1997;1320:107-41 pubmed
  36. Creaghan I, Guest J. Suppression of the succinate requirement of lipoamide dehydrogenase mutants of Escherichia coli by mutations affecting succinate dehydrogenase activity. J Gen Microbiol. 1977;102:183-94 pubmed
  37. Tran Q, Rothery R, Maklashina E, Cecchini G, Weiner J. Escherichia coli succinate dehydrogenase variant lacking the heme b. Proc Natl Acad Sci U S A. 2007;104:18007-12 pubmed
    ..In addition, the heme does not appear to be involved in reactive oxygen species suppression. Our results indicate that redox cycling of the heme in complex II is not essential for the enzyme's ubiquinol reductase activity. ..
  38. Gunsalus R, Park S. Aerobic-anaerobic gene regulation in Escherichia coli: control by the ArcAB and Fnr regulons. Res Microbiol. 1994;145:437-50 pubmed
    ..Together, they coordinate gene expression to adjust carbon flow with electron flow and energy generation so that cells can balance growth in an efficiently coupled manner. ..
  39. Yankovskaya V, Horsefield R, T rnroth S, Luna Chavez C, Miyoshi H, L ger C, et al. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 2003;299:700-4 pubmed publisher
    ..Furthermore, symptoms of genetic disorders associated with mitochondrial SQR mutations may be a result of ROS formation resulting from impaired electron transport in the enzyme...
  40. Nihei C, Nakayashiki T, Nakamura K, Inokuchi H, Gennis R, Kojima S, et al. Abortive assembly of succinate-ubiquinone reductase (complex II) in a ferrochelatase-deficient mutant of Escherichia coli. Mol Genet Genomics. 2001;265:394-404 pubmed
    ..coli, and provide a new insight into the biological role of heme in the molecular assembly of the multi-subunit enzyme complex. ..
  41. Spencer M, Guest J. Proteins of the inner membrane of Escherichia coli: identification of succinate dehydrogenase by polyacrylamide gel electrophoresis with sdh amber mutants. J Bacteriol. 1974;117:947-53 pubmed
    ..The band corresponded to a protein with a molecular weight of 67,000 daltons, which is close to that for the large subunits of the succinate dehydrogenases of Rhodospirillum rubrum and beef heart mitochondria. ..
  42. Cunningham L, Guest J. Transcription and transcript processing in the sdhCDAB-sucABCD operon of Escherichia coli. Microbiology. 1998;144 ( Pt 8):2113-23 pubmed
    ..Other sites of endonuclease processing were located by interpreting the patterns of transcript subfragments observed in Northern blotting. ..
  43. Creaghan I, Guest J. Succinate dehydrogenase-dependent nutritional requirement for succinate in mutants of Escherichia coli K12. J Gen Microbiol. 1978;107:1-13 pubmed
    ..Anaerobically, either isocitrate lyase or fumarate reductase is essential for succinate-independent growth on glucose. ..
  44. Horsefield R, Yankovskaya V, Sexton G, Whittingham W, Shiomi K, Omura S, et al. Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction. J Biol Chem. 2006;281:7309-16 pubmed
    ..This allows us to propose a mechanism for the reduction of ubiquinone during the catalytic turnover of the enzyme. ..
  45. Maklashina E, Iverson T, Sher Y, Kotlyar V, Andréll J, Mirza O, et al. Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain. J Biol Chem. 2006;281:11357-65 pubmed
    ..there is a Glu (FrdA Glu-49) near the covalently bound FAD cofactor in most QFRs, which is replaced with a Gln (SdhA Gln-50) in SQRs...
  46. Törnroth S, Yankovskaya V, Cecchini G, Iwata S. Purification, crystallisation and preliminary crystallographic studies of succinate:ubiquinone oxidoreductase from Escherichia coli. Biochim Biophys Acta. 2002;1553:171-6 pubmed
    ..coli QFR (fumarate reductase) as a search model. The packing suggests that E. coli SQR is a crystallographic trimer rather than a dimer as observed for the E. coli QFR. ..
  47. Kenney W, Walker W, Singer T. Studies on succinate dehydrogenase. XX. Amino acid sequence around the flavin site. J Biol Chem. 1972;247:4510-3 pubmed
  48. Darlison M, Guest J. Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli. Biochem J. 1984;223:507-17 pubmed
    ..It is separated by a 15 base-pair intergenic region from the preceding flavoprotein gene (sdhA) and is the distal gene of an operon that also includes genes (sdhC and D) encoding two hydrophobic subunits, ..
  49. Maklashina E, Berthold D, Cecchini G. Anaerobic expression of Escherichia coli succinate dehydrogenase: functional replacement of fumarate reductase in the respiratory chain during anaerobic growth. J Bacteriol. 1998;180:5989-96 pubmed
    ..coli accommodates the excess SQR produced by increasing the amount of membrane. The excess membrane was found in tubular structures that could be seen in thin-section electron micrographs. ..
  50. Anderson R, Hille R, Shinde S, Cecchini G. Electron transfer within complex II. Succinate:ubiquinone oxidoreductase of Escherichia coli. J Biol Chem. 2005;280:33331-7 pubmed
  51. Horsefield R, Yankovskaya V, Törnroth S, Luna Chavez C, Stambouli E, Barber J, et al. Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone oxidoreductase from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2003;59:600-2 pubmed
    ..7, c = 521.9 A, and diffract to 2.6 A resolution. The optimization strategy used for obtaining well diffracting SQR crystals is applicable to a wide range of membrane proteins. ..
  52. Brandsch R, Bichler V. Covalent cofactor binding to flavoenzymes requires specific effectors. Eur J Biochem. 1989;182:125-8 pubmed
    ..Our results suggest that covalent modification and thus activation of these enzymes is dependent on specific metabolic intermediates which may act as allosteric effectors in the reaction. ..
  53. Hagerhall C, Hederstedt L. A structural model for the membrane-integral domain of succinate: quinone oxidoreductases. FEBS Lett. 1996;389:25-31 pubmed
    ..The structure can be applied to a larger group of membrane-integral cytochromes of b-type and has evolutionary and functional implications. ..
  54. Cecchini G, Maklashina E, Yankovskaya V, Iverson T, Iwata S. Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases. FEBS Lett. 2003;545:31-8 pubmed
    ..These results suggest that the anaerobic and aerobic forms of complex II have evolved different mechanisms for electron and proton transfer in their respective membrane domains. ..
  55. Hederstedt L, Rutberg L. Succinate dehydrogenase--a comparative review. Microbiol Rev. 1981;45:542-55 pubmed
  56. Park S, Chao G, Gunsalus R. Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter. J Bacteriol. 1997;179:4138-42 pubmed
    ..These findings establish that the differential expression of eight genes for three of the TCA cycle enzymes in E. coli is controlled from one regulatory element. ..
  57. Pershad H, Hirst J, Cochran B, Ackrell B, Armstrong F. Voltammetric studies of bidirectional catalytic electron transport in Escherichia coli succinate dehydrogenase: comparison with the enzyme from beef heart mitochondria. Biochim Biophys Acta. 1999;1412:262-72 pubmed
    ..Thus, succinate dehydrogenase is an excellent fumarate reductase, but its activity in this direction is limited to a very specific range of potential. ..
  58. Echtenkamp P, Wilson D, Shuler M. Cell cycle progression in Escherichia coli B/r affects transcription of certain genes: Implications for synthetic genome design. Biotechnol Bioeng. 2009;102:902-9 pubmed publisher
    ..In conclusion, gene position, with regard to the C period, and gene function are important factors to incorporate into design criteria for synthetic bacterial genomes. ..