frdB

Summary

Gene Symbol: frdB
Description: fumarate reductase (anaerobic), Fe-S subunit
Alias: ECK4149, JW4114
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Luna Chavez C, Iverson T, Rees D, Cecchini G. Overexpression, purification, and crystallization of the membrane-bound fumarate reductase from Escherichia coli. Protein Expr Purif. 2000;19:188-96 pubmed
    ..6 A, b = 138.1 A, and c = 275.3 A. The purification and crystallization procedures are highly reproducible and the general procedure may prove useful for Complex IIs from other sources. ..
  2. Huang C, Lin X, Wu L, Zhang D, Liu D, Wang S, et al. Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins. J Proteome Res. 2006;5:3268-76 pubmed
    ..This established complete proteomic profile of E. coli envelope also sheds new insight into the function(s) of E. coli outer envelope. ..
  3. Hudson J, Heffron K, Kotlyar V, Sher Y, Maklashina E, Cecchini G, et al. Electron transfer and catalytic control by the iron-sulfur clusters in a respiratory enzyme, E. coli fumarate reductase. J Am Chem Soc. 2005;127:6977-89 pubmed
  4. Yankovskaya V, Sablin S, Ramsay R, Singer T, Ackrell B, Cecchini G, et al. Inhibitor probes of the quinone binding sites of mammalian complex II and Escherichia coli fumarate reductase. J Biol Chem. 1996;271:21020-4 pubmed
    ..The results were analyzed in terms of the model of these dual sites of quinone binding in fumarate reductase, as well as the nature of the substituent in the 2-position of the dinitrophenol inhibitors. ..
  5. Johnson M, Kowal A, Morningstar J, Oliver M, Whittaker K, Gunsalus R, et al. Subunit location of the iron-sulfur clusters in fumarate reductase from Escherichia coli. J Biol Chem. 1988;263:14732-8 pubmed
    ..These new results are discussed in light of the amino acid sequences of the two subunits and the sequences of structurally well characterized iron-sulfur proteins containing [2Fe-2S], [3Fe-4S], and [4Fe-4S] centers. ..
  6. Iverson T, Luna Chavez C, Croal L, Cecchini G, Rees D. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J Biol Chem. 2002;277:16124-30 pubmed publisher
    ..This acidic residue, Glu-C29, in the E. coli enzyme may act as a proton shuttle from the quinol during enzyme turnover...
  7. 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. ..
  8. Condon C, Weiner J. Fumarate reductase of Escherichia coli: an investigation of function and assembly using in vivo complementation. Mol Microbiol. 1988;2:43-52 pubmed
    ..Thus separation of the DNA coding for the FRD C and FRD D proteins affected the ability of fumarate reductase to assemble into a functional complex. ..
  9. Iverson T, Luna Chavez C, Schröder I, Cecchini G, Rees D. Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex. Curr Opin Struct Biol. 2000;10:448-55 pubmed
    ..These structures revealed the cofactor organization linking the fumarate and quinol sites, and showed a cofactor arrangement across the membrane that is suggestive of a possible energy coupling function. ..

More Information

Publications48

  1. Tseng C, Hansen A, Cotter P, Gunsalus R. Effect of cell growth rate on expression of the anaerobic respiratory pathway operons frdABCD, dmsABC, and narGHJI of Escherichia coli. J Bacteriol. 1994;176:6599-605 pubmed
    ..The cell appears to have many ways to adjust cell respiration in response to changes in cell growth conditions. ..
  2. Cecchini G, Sices H, Schröder I, Gunsalus R. Aerobic inactivation of fumarate reductase from Escherichia coli by mutation of the [3Fe-4S]-quinone binding domain. J Bacteriol. 1995;177:4587-92 pubmed
    ..A site-directed mutation of E. coli fumarate reductase in which FrdB Pro-159 was replaced with a glutamine or histidine residue was constructed and overexpressed in a strain of E...
  3. Westenberg D, Gunsalus R, Ackrell B, Sices H, Cecchini G. Escherichia coli fumarate reductase frdC and frdD mutants. Identification of amino acid residues involved in catalytic activity with quinones. J Biol Chem. 1993;268:815-22 pubmed
    ..The hydrophobic FrdC and FrdD subunits anchor the FrdA and FrdB catalytic subunits to the inner surface of the cytoplasmic membrane and are required for the enzyme to interact ..
  4. Grundstrom T, Jaurin B. Overlap between ampC and frd operons on the Escherichia coli chromosome. Proc Natl Acad Sci U S A. 1982;79:1111-5 pubmed
    ..C insertion in the promoter gave both increased transcription of ampC and a frameshift in this overlapping gene, resulting in readthrough proteins. Thus, we describe a type of very compact genetic organization of operons in prokaryotes. ..
  5. Tseng C, Albrecht J, Gunsalus R. Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli. J Bacteriol. 1996;178:1094-8 pubmed
    ..These two transcriptional regulators coordinate the hierarchial control of respiratory pathway gene expression in E. coli to ensure the optimal use of oxygen in the cell environment. ..
  6. Hagerhall C. Succinate: quinone oxidoreductases. Variations on a conserved theme. Biochim Biophys Acta. 1997;1320:107-41 pubmed
  7. 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. ..
  8. 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...
  9. Leger C, Heffron K, Pershad H, Maklashina E, Luna Chavez C, Cecchini G, et al. Enzyme electrokinetics: energetics of succinate oxidation by fumarate reductase and succinate dehydrogenase. Biochemistry. 2001;40:11234-45 pubmed
    ..Importantly, comparisons are made with the electrocatalytic properties of SDH, the membrane-extrinsic catalytic domain of mitochondrial complex II. ..
  10. Johnson M, Morningstar J, Cecchini G, Ackrell B. Detection of a tetranuclear iron-sulfur center in fumarate reductase from Escherichia coli by electron paramagnetic resonance spectroscopy. Biochem Biophys Res Commun. 1985;131:756-62 pubmed
    ..The observed enhancement of the spin relaxation of the [2Fe-2S]1+ cluster on dithionite reduction is attributed to spin-spin interaction between the S = 1/2, reduced tetranuclear and binuclear clusters. ..
  11. Blaut M, Whittaker K, Valdovinos A, Ackrell B, Gunsalus R, Cecchini G. Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin. J Biol Chem. 1989;264:13599-604 pubmed
    ..the FrdA subunit, which contains the active site, and a FAD prosthetic group covalently attached to His44, plus the FrdB subunit which contains at least two of the three nonidentical iron-sulfur clusters of the enzyme...
  12. Maklashina E, Hellwig P, Rothery R, Kotlyar V, Sher Y, Weiner J, et al. Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli. J Biol Chem. 2006;281:26655-64 pubmed
    ..These findings represent an example of how enzymes that are designed to accommodate either UQ or MQ at a single Q binding site may nevertheless develop sufficient plasticity at the binding pocket to react differently with MQ and UQ. ..
  13. Dickie P, Weiner J. Purification and characterization of membrane-bound fumarate reductase from anaerobically grown Escherichia coli. Can J Biochem. 1979;57:813-21 pubmed
    ..This would indicate that the enzyme is a dimer. The purified enzyme has low, but measurable, succinate dehydrogenase activity. ..
  14. Iverson T, Luna Chavez C, Cecchini G, Rees D. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 1999;284:1961-6 pubmed
    ..Although fumarate reductase is not associated with any proton-pumping function, the two quinones are positioned on opposite sides of the membrane in an arrangement similar to that of the Q-cycle organization observed for cytochrome bc1...
  15. Hirsch C, Rasminsky M, Davis B, Lin E. A FUMARATE REDUCTASE IN ESCHERICHIA COLI DISTINCT FROM SUCCINATE DEHYDROGENASE. J Biol Chem. 1963;238:3770-4 pubmed
  16. Seaver L, Imlay J. Are respiratory enzymes the primary sources of intracellular hydrogen peroxide?. J Biol Chem. 2004;279:48742-50 pubmed
    ..That source has not yet been identified. In respiring cells the rate of H2O2 production was approximately 0.5% the rate of total oxygen consumption, with only modest changes when cells used different carbon sources. ..
  17. Rothery R, Seime A, Spiers A, Maklashina E, Schröder I, Gunsalus R, et al. Defining the Q-site of Escherichia coli fumarate reductase by site-directed mutagenesis, fluorescence quench titrations and EPR spectroscopy. FEBS J. 2005;272:313-26 pubmed
    ..quench titrations, EPR spectroscopy and steady-state kinetics to study the effects of site-directed mutants of FrdB, FrdC and FrdD on the proximal menaquinol (MQH(2)) binding site (Q(P)) of Escherichia coli fumarate reductase (..
  18. Cole S, Guest J. Production of a soluble form of fumarate reductase by multiple gene duplication in Escherichia coli K12. Eur J Biochem. 1979;102:65-71 pubmed
    ..Production of the soluble form occurred when the binding capacity of the membrane was saturated. Both forms of fumarate reductase were enzymically active but the soluble form was readily inactivated under assay conditions. ..
  19. Lemire B, Robinson J, Weiner J. Identification of membrane anchor polypeptides of Escherichia coli fumarate reductase. J Bacteriol. 1982;152:1126-31 pubmed
    ..Unlike the well-characterized two-subunit form, the holoenzyme is not dependent on anions for activity and is not labile at alkaline pH. In these respects, it more closely resembles the membrane-bound activity. ..
  20. 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. ..
  21. Grundstrom T, Jaurin B, Edlund T, Normark S. Physical mapping and expression of hybrid plasmids carrying chromosomal beta-lactamase genes of Escherichia coli K-12. J Bacteriol. 1980;143:1127-34 pubmed
    ..Two second-step regulatory mutations mapped within the same 370-base pair region as ampA1. This piece of deoxyribonucleic acid therefore contains ampA, a control sequence region for ampC. ..
  22. Cecchini G, Ackrell B, Deshler J, Gunsalus R. Reconstitution of quinone reduction and characterization of Escherichia coli fumarate reductase activity. J Biol Chem. 1986;261:1808-14 pubmed
  23. Cohen Ben Lulu G, Francis N, Shimoni E, Noy D, Davidov Y, Prasad K, et al. The bacterial flagellar switch complex is getting more complex. EMBO J. 2008;27:1134-44 pubmed publisher
  24. Manodori A, Cecchini G, Schröder I, Gunsalus R, Werth M, Johnson M. [3Fe-4S] to [4Fe-4S] cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis. Biochemistry. 1992;31:2703-12 pubmed
    Site-directed mutants of Escherichia coli fumarate reductase in which FrdB Cys204, Cys210, and Cys214 were individually replaced by Ser and in which Val207 was replaced by Cys were constructed and overexpressed in a strain of E...
  25. 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
  26. Latour D, Weiner J. Assembly of Escherichia coli fumarate reductase holoenzyme. Biochem Cell Biol. 1989;67:251-9 pubmed
    ..and FrdD, the membrane anchor polypeptides, assembled rapidly into the membrane and then were capped with FrdA and FrdB in separate events...
  27. Kowal A, Werth M, Manodori A, Cecchini G, Schröder I, Gunsalus R, et al. Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase. Biochemistry. 1995;34:12284-93 pubmed
    Site-directed mutants of Escherichia coli fumarate reductase in which FrdB Cys148, Cys151, Cys154, and Cys158 are replaced individually by Ser have been constructed and overexpressed in a strain of E...
  28. Cole S, Guest J. Amplification of fumarate reductase synthesis with lambdafrdA transducing phages and orientation of frdA gene expression. Mol Gen Genet. 1980;179:377-85 pubmed
  29. 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. ..
  30. Cole S, Grundstrom T, Jaurin B, Robinson J, Weiner J. Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli. Eur J Biochem. 1982;126:211-6 pubmed
    The frdB gene, encoding the iron-sulphur protein subunit of fumarate reductase, has been located and its complete nucleotide sequence determined...
  31. Cole S, Condon C, Lemire B, Weiner J. Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli. Biochim Biophys Acta. 1985;811:381-403 pubmed
  32. Jones H, Gunsalus R. Transcription of the Escherichia coli fumarate reductase genes (frdABCD) and their coordinate regulation by oxygen, nitrate, and fumarate. J Bacteriol. 1985;164:1100-9 pubmed
  33. Johnson M, Morningstar J, Cecchini G, Ackrell B. In vivo detection of a three iron cluster in fumarate reductase from Escherichia coli. Biochem Biophys Res Commun. 1985;131:653-8 pubmed
    ..The significance of this observation is discussed in relation to the physiological relevance of trinuclear iron-sulfur clusters. ..
  34. Ackrell B, Cochran B, Cecchini G. Interactions of oxaloacetate with Escherichia coli fumarate reductase. Arch Biochem Biophys. 1989;268:26-34 pubmed
    ..The reason for the difference is not known. The redox potential of the FAD/FADH2 couple in FRD (Em approximately -55 mV) was also slightly more positive than that in cardiac succinate dehydrogenase (-90 mV). ..
  35. Werth M, Cecchini G, Manodori A, Ackrell B, Schröder I, Gunsalus R, et al. Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster. Proc Natl Acad Sci U S A. 1990;87:8965-9 pubmed
    ..mutants of Escherichia coli fumarate reductase in which each of the four N-terminal cysteine residues in the FrdB subunit, residues 57, 62, 65, and 77, was mutated individually to serine have been constructed, overexpressed, and ..
  36. 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
  37. Weiner J, Cammack R, Cole S, Condon C, Honore N, Lemire B, et al. A mutant of Escherichia coli fumarate reductase decoupled from electron transport. Proc Natl Acad Sci U S A. 1986;83:2056-60 pubmed
    ..These results confirm the important role of the anchor subunits in functional electron transport and have implications for communication between intrinsic and extrinsic domains of membrane proteins. ..
  38. Lohmeier E, Hagen D, Dickie P, Weiner J. Cloning and expression of fumarate reductase gene of Escherichia coli. Can J Biochem. 1981;59:158-64 pubmed
    ..Regulation of plasmid-encoded enzyme, like the chromosomally encoded enzyme, is dependent upon the presence of fumarate and anaerobiosis. ..
  39. Sucheta A, Cammack R, Weiner J, Armstrong F. Reversible electrochemistry of fumarate reductase immobilized on an electrode surface. Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport. Biochemistry. 1993;32:5455-65 pubmed
    ..This small boost to the catalytic current indicates that the low-potential [4Fe-4S] cluster can function as a second center for relaying electrons to the FAD. ..