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Gene Review

frdB  -  fumarate reductase iron-sulfur subunit

Escherichia coli CFT073

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Disease relevance of frdB

  • The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex [1].
  • New properties of Bacillus subtilis succinate dehydrogenase altered at the active site. The apparent active site thiol of succinate oxidoreductases is dispensable for succinate oxidation [2].
  • The use of these procedures to fractionate membrane components from Haemophilus influenzae type b strains H-2 and H-E led to good separation of outer- and inner-membrane-enriched fractions as determined by succinate dehydrogenase and ketodeoxyoctonate levels but incomplete separation as determined by polyacrylamide gradient gel electrophoresis [3].
  • The sdhCDAB operon, encoding succinate dehydrogenase, was cloned from the soybean symbiont Bradyrhizobium japonicum [4].
  • Characterization of the succinate dehydrogenase-encoding gene cluster (sdh) from the rickettsia Coxiella burnetii [5].

High impact information on frdB

  • The homologous enzyme succinate dehydrogenase also plays a prominent role in cellular energetics as a member of the Krebs cycle and as complex II of the aerobic respiratory chain [6].
  • RyhB RNA levels are inversely correlated with mRNA levels for the sdhCDAB operon, encoding succinate dehydrogenase, as well as five other genes previously shown to be positively regulated by Fur by an unknown mechanism [7].
  • After in vitro transcription and translation, the preprotein was efficiently imported into isolated yeast mitochondria, cleaved to its mature form, and assembled into the membrane-bound succinate dehydrogenase complex [8].
  • SQR, often referred to as Complex II or succinate dehydrogenase, is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol (QH(2)) [9].
  • We have examined the role of the quinone-binding (Q(P)) site of Escherichia coli succinate:ubiquinone oxidoreductase (succinate dehydrogenase) in heme reduction and reoxidation during enzyme turnover [10].

Chemical compound and disease context of frdB

  • However, the cytochrome b556 in E. coli SdhC-SdhD fraction is reducible by succinate in the presence of mitochondrial succinate dehydrogenase, and the rate of cytochrome b556 reduction correlates with the reconstitutive activity of the mitochondrial succinate dehydrogenase [11].
  • The Iron-Sulfur Clusters in Escherichia coli Succinate Dehydrogenase Direct Electron Flow [12].
  • Longer (60 min) exposure of E. coli to the myeloperoxidase system resulted in only modest further inhibition of the ubiquinol oxidase, but the ubiquinol to total quinone ratio fell to 0%, reflecting complete loss of succinate dehydrogenase activity [13].
  • An invariant arginine in juxtaposition to Ala-252 in the flavoprotein of B. subtilis SDH, and to the invariant cysteine in the E. coli homologous enzymes, is probably essential for substrate binding [2].
  • In contrast, authentic fumarate reductases of anaerobic cells (and 'succinate dehydrogenase' from Bacillus subtilis) neither exhibit the electrochemical effect nor deviate from simple kinetic behaviour in the cuvette assay [14].

Biological context of frdB

  • Consideration of the ESR properties of this signal, together with the amino acid sequence of the frdB subunit of the enzyme, indicates that Centre 2 is a [4Fe-4S] cluster which, in its reduced state, enhances the spin relaxation of the [2Fe-2S] Centre 1 [15].
  • Succinate dehydrogenase is an indispensable enzyme involved in the Krebs cycle as well as energy coupling in the mitochondria and certain prokaryotes [12].
  • In the present study, to elucidate the role of two hydrophobic subunits in the heme b ligation and functional assembly of complex II, plasmids carrying portions of the sdh gene were constructed and introduced into E. coli MK3, which lacks succinate dehydrogenase and fumarate reductase activities [16].
  • To examine how the sdhCDAB genes that encode SDH are regulated by changes in the environment, sdh-lacZ fusions were constructed and analysed in vivo following cell growth under a variety of alternative culture conditions [17].
  • Previous studies have established that succinate dehydrogenase (SDH) synthesis is elevated by aerobiosis and suppressed during growth with glucose [17].

Anatomical context of frdB


Associations of frdB with chemical compounds


Other interactions of frdB

  • Sequencing studies of a region centered approx. 5.6 kb upstream from gltA revealed an ORF read with opposite polarity that encodes a peptide highly homologous to the C terminus of the flavoprotein subunit of E. coli succinate dehydrogenase [28].

Analytical, diagnostic and therapeutic context of frdB


  1. The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex. Condon, C., Cammack, R., Patil, D.S., Owen, P. J. Biol. Chem. (1985) [Pubmed]
  2. New properties of Bacillus subtilis succinate dehydrogenase altered at the active site. The apparent active site thiol of succinate oxidoreductases is dispensable for succinate oxidation. Hederstedt, L., Hedén, L.O. Biochem. J. (1989) [Pubmed]
  3. Induction of active immunity with membrane fractions from Haemophilus influenzae type b. Burans, J.P., Lynn, M., Solotorovsky, M. Infect. Immun. (1983) [Pubmed]
  4. Succinate dehydrogenase (Sdh) from Bradyrhizobium japonicum is closely related to mitochondrial Sdh. Westenberg, D.J., Guerinot, M.L. J. Bacteriol. (1999) [Pubmed]
  5. Characterization of the succinate dehydrogenase-encoding gene cluster (sdh) from the rickettsia Coxiella burnetii. Heinzen, R.A., Mo, Y.Y., Robertson, S.J., Mallavia, L.P. Gene (1995) [Pubmed]
  6. Structure of the Escherichia coli fumarate reductase respiratory complex. Iverson, T.M., Luna-Chavez, C., Cecchini, G., Rees, D.C. Science (1999) [Pubmed]
  7. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Massé, E., Gottesman, S. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  8. Primary structure, import, and assembly of the yeast homolog of succinate dehydrogenase flavoprotein. Schülke, N., Blobel, G., Pain, D. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. 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. Horsefield, R., Yankovskaya, V., Sexton, G., Whittingham, W., Shiomi, K., Omura, S., Byrne, B., Cecchini, G., Iwata, S. J. Biol. Chem. (2006) [Pubmed]
  10. The Quinone Binding Site in Escherichia coli Succinate Dehydrogenase Is Required for Electron Transfer to the Heme b. Tran, Q.M., Rothery, R.A., Maklashina, E., Cecchini, G., Weiner, J.H. J. Biol. Chem. (2006) [Pubmed]
  11. Resolution and reconstitution of succinate-ubiquinone reductase from Escherichia coli. Yang, X., Yu, L., Yu, C.A. J. Biol. Chem. (1997) [Pubmed]
  12. The Iron-Sulfur Clusters in Escherichia coli Succinate Dehydrogenase Direct Electron Flow. Cheng, V.W., Ma, E., Zhao, Z., Rothery, R.A., Weiner, J.H. J. Biol. Chem. (2006) [Pubmed]
  13. Myeloperoxidase-mediated inhibition of microbial respiration: damage to Escherichia coli ubiquinol oxidase. Rakita, R.M., Michel, B.R., Rosen, H. Biochemistry (1989) [Pubmed]
  14. Classification of fumarate reductases and succinate dehydrogenases based upon their contrasting behaviour in the reduced benzylviologen/fumarate assay. Ackrell, B.A., Armstrong, F.A., Cochran, B., Sucheta, A., Yu, T. FEBS Lett. (1993) [Pubmed]
  15. Evidence that centre 2 in Escherichia coli fumarate reductase is a [4Fe-4S]cluster. Cammack, R., Patil, D.S., Weiner, J.H. Biochim. Biophys. Acta (1986) [Pubmed]
  16. Two hydrophobic subunits are essential for the heme b ligation and functional assembly of complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli. Nakamura, K., Yamaki, M., Sarada, M., Nakayama, S., Vibat, C.R., Gennis, R.B., Nakayashiki, T., Inokuchi, H., Kojima, S., Kita, K. J. Biol. Chem. (1996) [Pubmed]
  17. Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr. Park, S.J., Tseng, C.P., Gunsalus, R.P. Mol. Microbiol. (1995) [Pubmed]
  18. Isolation and characterization of a Saccharomyces cerevisiae mutant disrupted for the succinate dehydrogenase flavoprotein subunit. Robinson, K.M., von Kieckebusch-Gück, A., Lemire, B.D. J. Biol. Chem. (1991) [Pubmed]
  19. Cloning and expression in Escherichia coli of sdhA, the structural gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex. Magnusson, K., Hederstedt, L., Rutberg, L. J. Bacteriol. (1985) [Pubmed]
  20. Analysis of mitochondrial antigens reveals inner membrane succinate dehydrogenase flavoprotein subunit as autoantigen to antibodies in anti-M7 sera. Cicek, G., Schiltz, E., Hess, D., Staiger, J., Brandsch, R. Clin. Exp. Immunol. (2002) [Pubmed]
  21. Modification of bovine heart succinate dehydrogenase with ethoxyformic anhydride and rose bengal: evidence for essential histidyl residues protectable by substrates. Hederstedt, L., Hatefi, Y. Arch. Biochem. Biophys. (1986) [Pubmed]
  22. Covalent cofactor binding to flavoenzymes requires specific effectors. Brandsch, R., Bichler, V. Eur. J. Biochem. (1989) [Pubmed]
  23. Investigation of Escherichia coli fumarate reductase subunit function using transposon Tn5. Latour, D.J., Weiner, J.H. J. Gen. Microbiol. (1987) [Pubmed]
  24. Isolation and nucleotide sequence of the Saccharomyces cerevisiae gene for the succinate dehydrogenase flavoprotein subunit. Robinson, K.M., Lemire, B.D. J. Biol. Chem. (1992) [Pubmed]
  25. The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies. Oyedotun, K.S., Lemire, B.D. J. Biol. Chem. (2004) [Pubmed]
  26. Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis. Schröder, I., Gunsalus, R.P., Ackrell, B.A., Cochran, B., Cecchini, G. J. Biol. Chem. (1991) [Pubmed]
  27. Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. Messner, K.R., Imlay, J.A. J. Biol. Chem. (2002) [Pubmed]
  28. Sequence and linkage analysis of the Coxiella burnetii citrate synthase-encoding gene. Heinzen, R.A., Frazier, M.E., Mallavia, L.P. Gene (1991) [Pubmed]
  29. Cloning of toxic genes with mini-mu derivative of bacteriophage mu. Stuchlík, S., Janitorová, V., Turna, J. Acta Virol. (1993) [Pubmed]
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