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Escherichia coli K-12 substr. MG1655 Polypeptide: fumarate reductase iron-sulfur protein



Gene: frdB Accession Numbers: EG10331 (EcoCyc), b4153, ECK4149

Regulation Summary Diagram: ?

Component of: fumarate reductase (extended summary available)

Summary:
This is one of two catalytic subunits of the four subunit fumarate reductase complex. FrdB contains 11 cysteine residues arranged in three clusters predicted to form the iron-sulfur clusters [Cole82a]. This subunit contains three iron-sulfur clusters: a 4Fe-4S, a 3Fe-4S and a 2Fe-2S [Iverson99].

This subunit has 38% identity to the succinate dehydrogenase iron-sulfur binding subunit, SdhB [Darlison84a].

Gene Citations: [Tseng94, Tseng96]

Locations: inner membrane, cytosol

Map Position: [4,377,806 <- 4,378,540] (94.36 centisomes)
Length: 735 bp / 244 aa

Molecular Weight of Polypeptide: 27.123 kD (from nucleotide sequence), 27.0 kD (experimental) [Cole82a ]

pI: 6.46

Unification Links: ASAP:ABE-0013602 , CGSC:741 , EchoBASE:EB0327 , EcoGene:EG10331 , EcoliWiki:b4153 , OU-Microarray:b4153 , PortEco:frdB , PR:PRO_000022687 , Pride:P0AC47 , Protein Model Portal:P0AC47 , RefSeq:NP_418577 , RegulonDB:EG10331 , SMR:P0AC47 , String:511145.b4153 , UniProt:P0AC47

Relationship Links: InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR004489 , InterPro:IN-FAMILY:IPR006058 , InterPro:IN-FAMILY:IPR009051 , InterPro:IN-FAMILY:IPR012285 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , InterPro:IN-FAMILY:IPR025192 , PDB:Structure:1KF6 , PDB:Structure:1KFY , PDB:Structure:1L0V , PDB:Structure:2B76 , PDB:Structure:3CIR , PDB:Structure:3P4P , PDB:Structure:3P4Q , PDB:Structure:3P4R , PDB:Structure:3P4S , Pfam:IN-FAMILY:PF13085 , Pfam:IN-FAMILY:PF13183 , Prosite:IN-FAMILY:PS00197 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51379

In Paralogous Gene Group: 185 (2 members)

Reactions known to consume the compound:

Not in pathways:
a reduced flavoprotein (FMNH2) + an iron-sulfur protein → an oxidized flavoprotein (FMN) + a reduced iron-sulfur protein + 2 H+

Reactions known to produce the compound:

Not in pathways:
a menaquinone oxidoreductase (menaquinone-8) + a reduced iron-sulfur protein + 2 H+ → a menaquinone oxidoreductase (menaquinol-8) + an iron-sulfur protein + 2 H+
a menaquinone oxidoreductase (demethylmenaquinone) + a reduced iron-sulfur protein + 2 H+ → a menaquinone oxidoreductase (demethylmenaquinol) + an iron-sulfur protein + 2 H+
a reduced iron-sulfur protein + a ubiquinone-8 oxidoreductase + 2 H+an iron-sulfur protein + a ubiquinol-8 oxidoreductase + 2 H+

In Reactions of unknown directionality:

Not in pathways:
an iron-sulfur protein + 2 e- = a reduced iron-sulfur protein

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0001539 - cilium or flagellum-dependent cell motility Inferred from experiment [CohenBenLulu08]
GO:0006113 - fermentation Inferred from experiment [Hirsch63]
GO:0009061 - anaerobic respiration Inferred from experiment [Condon88, Hirsch63]
GO:0044780 - bacterial-type flagellum assembly Inferred from experiment [CohenBenLulu08]
GO:0006099 - tricarboxylic acid cycle Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0000104 - succinate dehydrogenase activity Inferred from experiment [Lemire82]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Lasserre06, Iverson02, Huang06]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01a, Leger01, Sucheta93]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Iverson99]
GO:0051538 - 3 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Iverson99]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Iverson99]
GO:0008177 - succinate dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01a, Cole82a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Lemire82, Iverson99]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0045284 - plasma membrane fumarate reductase complex Inferred from experiment [Lemire82, Iverson99]

MultiFun Terms: metabolism energy metabolism, carbon anaerobic respiration
metabolism energy metabolism, carbon fermentation
metabolism energy production/transport electron acceptors

Essentiality data for frdB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 28-Apr-2008 by Nolan L , Macquarie University


Subunit of: fumarate reductase

Synonyms: menaquinol:fumarate oxidoreductase, FRD, QFR, fumarate reductase, quinol:fumarate oxidoreductase

Subunit composition of fumarate reductase = [FrdA][FrdB][FrdC][FrdD]
         fumarate reductase flavoprotein = FrdA (summary available)
         fumarate reductase iron-sulfur protein = FrdB (summary available)
         fumarate reductase membrane protein = FrdC (summary available)
         fumarate reductase membrane protein = FrdD (summary available)

Summary:
Quinol:fumarate oxidoreductase (QFR) or fumarate reductase or is a membrane bound flavoprotein that catalyses the reduction of fumarate to succinate under anaerobic conditions [Hirsch63]. QFR is a respiratory enzyme - it is one of a number of reductases that function as terminal electron acceptors during anaerobic respiration in E. coli K-12 (reviewed by [Unden97].

Functional QFR is essential for anaerobic growth on glycerol, lactate or formate when fumarate serves as the terminal electron acceptor. It is also essential for anaerobic H2 dependent growth with fumarate. Menaquinone is the obligatory electron donor [Spencer73a, Lambden76, Wissenbach90]. Anaerobic growth of E. coli K-12 with fumarate operates preferentially with NADH dehydrogenase I [Tran97]

Fumarate reductase is composed of 4 subunits; the complex contains a cytoplasmic catalytic domain - FrdAB - containing bound flavin cofactor and three iron-sulfur clusters and a membrane anchor domain (FrdCD) which contains the quinol binding site(s) [Weiner79, Lohmeier81, Lemire82, Morningstar85, Johnson85b, Johnson85a, Iverson99]. All 4 subunits are essential for anaerobic growth on glycerol and fumarate [Condon88]. The crystal structure of purified fumarate reductase contains two menaquinol molecules (Qp and Qd) bound on opposite sides of the membrane-spanning region; Qp is proximal to the site of fumarate reduction, Qd is distal. It is not clear whether both of the quinol-binding sites are functionally relevant [Iverson99, Iverson02, Iverson00, Rothery05]. The 6 redox cofactors are organised in a chain with the sequence FAD - 2Fe:2S - 4Fe:4S - 3Fe:4S - Qp - Qd [Iverson99].

QFR is structurally and functionally homologous to succinate dehydrogenase (SQR) which catalyses the oxidation of succinate to fumarate under aerobic conditions. The functions of QFR and SQR are partially interchangeable - a plasmid containing the frd genes is able to compensate for the growth deficiency of an sdh mutant [Guest81] while anaerobic expression of succinate dehydrogenase supports the growth of an frd mutant [Maklashina98].

A crystal structure of the purified complex indicated dimer formation but this is unlikely to be physiologically relevent [Iverson99].

Expression of the frd operon is repressed by the preferred electron acceptors, oxygen and nitrate and induced by fumarate [Jones85, Jones87a, Iuchi87].

QFR transmits the effects of fumarate (known to be a flagella switching factor in E. coli [Barak96, Prasad98]) to the flagella switch. Cells lacking QFR are defective in flagella assembly and switching of flagella rotation as well as being insensitive to fumarate. QFR interacts with the flagella switch protein FliG in vitro [CohenBenLulu08].

Reviews: [Cecchini02]
Comment: [Hederstedt99]

Citations: [Cole85, Guest79, Johnson85c, Salerno91, Lancaster00, Brandsch89, Tseng94, Kalman89, Kalman88, Goh05, Golby99, Latour88, Cecchini95, Rothery98, Cheng13, Manodori92, Kowal95, Singh13a, Maklashina06a, Dickie79, vanderPlas83]

Locations: inner membrane

Relationship Links: PDB:Structure:1KF6 , PDB:Structure:1KFY , PDB:Structure:1L0V

GO Terms:

Biological Process: GO:0001539 - cilium or flagellum-dependent cell motility Inferred from experiment [CohenBenLulu08]
GO:0006113 - fermentation Inferred from experiment [Hirsch63]
GO:0009061 - anaerobic respiration Inferred from experiment [Condon88, Hirsch63, Spencer73a, Lambden76]
GO:0019645 - anaerobic electron transport chain Inferred from experiment [Miki75]
GO:0044780 - bacterial-type flagellum assembly Inferred from experiment [CohenBenLulu08]
Molecular Function: GO:0000104 - succinate dehydrogenase activity Inferred by computational analysis Inferred from experiment [Lemire82, Hirsch63, GOA01]
GO:0005515 - protein binding Inferred from experiment [CohenBenLulu08]
GO:0008177 - succinate dehydrogenase (ubiquinone) activity Inferred from experiment [Lambden76]
GO:0009055 - electron carrier activity Inferred from experiment [Leger01, Sucheta93]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred from experiment [Morningstar85, Johnson85b, Iverson99]
GO:0051538 - 3 iron, 4 sulfur cluster binding Inferred from experiment [Johnson85a, Iverson99]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment [Johnson85b, Iverson99]
GO:0071949 - FAD binding Inferred from experiment [Weiner79]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [GOA00, GOA01a]
Cellular Component: GO:0005887 - integral component of plasma membrane Inferred from experiment [Lemire82]
GO:0045284 - plasma membrane fumarate reductase complex Inferred from experiment [Iverson99, Lemire82]

Credits:
Revised 27-Aug-2014 by Mackie A , Macquarie University
Last-Curated ? 27-Aug-2014 by Mackie A , Macquarie University


Enzymatic reaction of: fumarate reductase

Synonyms: QFR, menaquinol-fumarate oxidoreductase, FrdABCD, fumarate reductase

EC Number: 1.3.5.4

In Pathways: mixed acid fermentation , glycerol-3-phosphate to fumarate electron transfer , NADH to fumarate electron transfer

Citations: [LunaChavez00, Cole85]

Cofactors or Prosthetic Groups: a [4Fe-4S] iron-sulfur cluster , [2Fe-2S] iron-sulfur cluster , FAD , [3Fe-4S] iron-sulfur cluster

Inhibitors (Competitive): malonate [Maklashina99] , a 2-alkyl-dinitrophenol derivative [Comment 5] , a ubiquinol analogue [Comment 6] , pentachlorophenol [Maklashina99]

Inhibitors (Noncompetitive): a 2-alkyl-dinitrophenol derivative [Maklashina99, Comment 7] , 2-n-heptyl-4-hydroxyquinoline-N-oxide [Maklashina99]

Inhibitors (Unknown Mechanism): oxaloacetate [Iverson99]

Primary Physiological Regulators of Enzyme Activity: oxaloacetate , malonate

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
succinate
1.5
14.0
[Cecchini02, BRENDA14]
succinate
550.0
30.0
[Maklashina06, BRENDA14]
succinate
15.0
[Maklashina06a, BRENDA14]
fumarate
5.4
177.0
[Cecchini02, BRENDA14]
fumarate
230.0
[Maklashina06a, BRENDA14]
fumarate
20.0
250.0
[Maklashina06, BRENDA14]


Sequence Features

Feature Class Location Citations Comment State
Cleavage-of-Initial-Methionine 1
[UniProt10]
UniProt: Removed;
 
Chain 2 -> 244
[UniProt09]
UniProt: Fumarate reductase iron-sulfur subunit;
 
Conserved-Region 16 -> 97
[UniProt09]
UniProt: 2Fe-2S ferredoxin-type;
 
Metal-Binding-Site 58, 63, 66, 78
[Iverson99]
2Fe:2S coordination site
Bound
Mutagenesis-Variant 58
[UniProt10]
Alternate sequence: C → S; UniProt: Affects center 1 (2Fe-2S);
 
Metal-Binding-Site 58
[UniProt10, Cole82a]
UniProt: Iron-sulfur 1 (2Fe-2S);
 
Mutagenesis-Variant 63
[UniProt10]
Alternate sequence: C → S; UniProt: Affects center 1 (2Fe-2S);
 
Metal-Binding-Site 63
[UniProt10, Cole82a]
UniProt: Iron-sulfur 1 (2Fe-2S);
 
Mutagenesis-Variant 66
[UniProt10]
Alternate sequence: C → S; UniProt: Affects center 1 (2Fe-2S);
 
Metal-Binding-Site 66
[UniProt10, Cole82a]
UniProt: Iron-sulfur 1 (2Fe-2S);
 
Mutagenesis-Variant 78
[UniProt10]
Alternate sequence: C → S; UniProt: Affects center 1 (2Fe-2S);
 
Metal-Binding-Site 78
[UniProt10, Cole82a]
UniProt: Iron-sulfur 1 (2Fe-2S);
 
Conserved-Region 140 -> 169
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type;
 
Metal-Binding-Site 149, 152, 155, 215
[Iverson99]
4Fe:4S coordination site
Bound
Metal-Binding-Site 149
[UniProt10, Cole82a]
UniProt: Iron-sulfur 2 (4Fe-4S);
 
Metal-Binding-Site 152
[UniProt10, Cole82a]
UniProt: Iron-sulfur 2 (4Fe-4S);
 
Metal-Binding-Site 155
[UniProt10, Cole82a]
UniProt: Iron-sulfur 2 (4Fe-4S);
 
Metal-Binding-Site 159, 205, 211
[Iverson99]
3Fe:4S coordination site
Bound
Metal-Binding-Site 159
[UniProt10, Cole82a]
UniProt: Iron-sulfur 3 (3Fe-4S);
 
Metal-Binding-Site 205
[UniProt10, Cole82a]
UniProt: Iron-sulfur 3 (3Fe-4S);
 
Metal-Binding-Site 211
[UniProt10, Cole82a]
UniProt: Iron-sulfur 3 (3Fe-4S);
 
Metal-Binding-Site 215
[UniProt10, Cole82a]
UniProt: Iron-sulfur 2 (4Fe-4S);
 


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b4153 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10331; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Barak96: Barak R, Giebel I, Eisenbach M (1996). "The specificity of fumarate as a switching factor of the bacterial flagellar motor." Mol Microbiol 19(1);139-44. PMID: 8821943

Brandsch89: Brandsch R, Bichler V (1989). "Covalent cofactor binding to flavoenzymes requires specific effectors." Eur J Biochem 1989;182(1);125-8. PMID: 2659351

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Cecchini02: Cecchini G, Schroder I, Gunsalus RP, Maklashina E (2002). "Succinate dehydrogenase and fumarate reductase from Escherichia coli." Biochim Biophys Acta 1553(1-2);140-57. PMID: 11803023

Cecchini86: Cecchini G, Thompson CR, Ackrell BA, Westenberg DJ, Dean N, Gunsalus RP (1986). "Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide." Proc Natl Acad Sci U S A 83(23);8898-902. PMID: 3538014

Cecchini95: Cecchini G, Sices H, Schroder I, Gunsalus RP (1995). "Aerobic inactivation of fumarate reductase from Escherichia coli by mutation of the [3Fe-4S]-quinone binding domain." J Bacteriol 177(16);4587-92. PMID: 7642483

Cheng13: Cheng VW, Tran QM, Boroumand N, Rothery RA, Maklashina E, Cecchini G, Weiner JH (2013). "A conserved lysine residue controls iron-sulfur cluster redox chemistry in Escherichia coli fumarate reductase." Biochim Biophys Acta 1827(10);1141-7. PMID: 23711795

CohenBenLulu08: Cohen-Ben-Lulu GN, Francis NR, Shimoni E, Noy D, Davidov Y, Prasad K, Sagi Y, Cecchini G, Johnstone RM, Eisenbach M (2008). "The bacterial flagellar switch complex is getting more complex." EMBO J 27(7);1134-44. PMID: 18337747

Cole82a: Cole ST, Grundstrom T, Jaurin B, Robinson JJ, Weiner JH (1982). "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 126(1);211-6. PMID: 6751816

Cole85: Cole ST, Condon C, Lemire BD, Weiner JH (1985). "Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli." Biochim Biophys Acta 1985;811(4);381-403. PMID: 3910107

Condon88: Condon C, Weiner JH (1988). "Fumarate reductase of Escherichia coli: an investigation of function and assembly using in vivo complementation." Mol Microbiol 2(1);43-52. PMID: 3285122

Darlison84a: Darlison MG, Guest JR (1984). "Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli." Biochem J 1984;223(2);507-17. PMID: 6388571

Dickie79: Dickie P, Weiner JH (1979). "Purification and characterization of membrane-bound fumarate reductase from anaerobically grown Escherichia coli." Can J Biochem 57(6);813-21. PMID: 383238

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA00: GOA (2000). "Gene Ontology annotation based on Swiss-Prot keyword mapping."

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Goh05: Goh EB, Bledsoe PJ, Chen LL, Gyaneshwar P, Stewart V, Igo MM (2005). "Hierarchical control of anaerobic gene expression in Escherichia coli K-12: the nitrate-responsive NarX-NarL regulatory system represses synthesis of the fumarate-responsive DcuS-DcuR regulatory system." J Bacteriol 187(14);4890-9. PMID: 15995204

Golby99: Golby P, Davies S, Kelly DJ, Guest JR, Andrews SC (1999). "Identification and characterization of a two-component sensor-kinase and response-regulator system (DcuS-DcuR) controlling gene expression in response to C4-dicarboxylates in Escherichia coli." J Bacteriol 1999;181(4);1238-48. PMID: 9973351

Grundstrom80: Grundstrom T, Jaurin B, Edlund T, Normark S (1980). "Physical mapping and expression of hybrid plasmids carrying chromosomal beta-lactamase genes of Escherichia coli K-12." J Bacteriol 143(3);1127-34. PMID: 6251026

Guest79: Guest JR (1979). "Anaerobic growth of Escherichia coli K12 with fumarate as terminal electron acceptor. Genetic studies with menaquinone and fluoroacetate-resistant mutants." J Gen Microbiol 115(2);259-71. PMID: 393800

Guest81: Guest JR (1981). "Partial replacement of succinate dehydrogenase function by phage- and plasmid-specified fumarate reductase in Escherichia coli." J Gen Microbiol 122(Pt 2);171-9. PMID: 6274999

Hederstedt99: Hederstedt L (1999). "Respiration without O2." Science 284(5422);1941-2. PMID: 10400536

Hirsch63: Hirsch CA, Rasminsky M, Davis BD, Lin EC (1963). "A fumarate reductase in Escherichia coli distinct from succinate dehydrogenase." J Biol Chem 238;3770-4. PMID: 14109218

Huang06: Huang CZ, Lin XM, Wu LN, Zhang DF, Liu D, Wang SY, Peng XX (2006). "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 5(12);3268-76. PMID: 17137328

Iuchi87: Iuchi S, Lin EC (1987). "The narL gene product activates the nitrate reductase operon and represses the fumarate reductase and trimethylamine N-oxide reductase operons in Escherichia coli." Proc Natl Acad Sci U S A 1987;84(11);3901-5. PMID: 3035558

Iverson00: Iverson TM, Luna-Chavez C, Schroder I, Cecchini G, Rees DC (2000). "Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex." Curr Opin Struct Biol 10(4);448-55. PMID: 10981634

Iverson02: Iverson TM, Luna-Chavez C, Croal LR, Cecchini G, Rees DC (2002). "Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site." J Biol Chem 277(18);16124-30. PMID: 11850430

Iverson99: Iverson TM, Luna-Chavez C, Cecchini G, Rees DC (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex." Science 1999;284(5422);1961-6. PMID: 10373108

Johnson85a: Johnson MK, Morningstar JE, Cecchini G, Ackrell BA (1985). "In vivo detection of a three iron cluster in fumarate reductase from Escherichia coli." Biochem Biophys Res Commun 131(2);653-8. PMID: 2996520

Johnson85b: Johnson MK, Morningstar JE, Cecchini G, Ackrell BA (1985). "Detection of a tetranuclear iron-sulfur center in fumarate reductase from Escherichia coli by electron paramagnetic resonance spectroscopy." Biochem Biophys Res Commun 131(2);756-62. PMID: 2996525

Johnson85c: Johnson MK, Bennett DE, Morningstar JE, Adams MW, Mortenson LE (1985). "The iron-sulfur cluster composition of Escherichia coli nitrate reductase." J Biol Chem 260(9);5456-63. PMID: 2985594

Jones85: Jones HM, Gunsalus RP (1985). "Transcription of the Escherichia coli fumarate reductase genes (frdABCD) and their coordinate regulation by oxygen, nitrate, and fumarate." J Bacteriol 1985;164(3);1100-9. PMID: 2999070

Jones87a: Jones HM, Gunsalus RP (1987). "Regulation of Escherichia coli fumarate reductase (frdABCD) operon expression by respiratory electron acceptors and the fnr gene product." J Bacteriol 169(7);3340-9. PMID: 3298218

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kalman88: Kalman LV, Gunsalus RP (1988). "The frdR gene of Escherichia coli globally regulates several operons involved in anaerobic growth in response to nitrate." J Bacteriol 170(2);623-9. PMID: 3276662

Kalman89: Kalman LV, Gunsalus RP (1989). "Identification of a second gene involved in global regulation of fumarate reductase and other nitrate-controlled genes for anaerobic respiration in Escherichia coli." J Bacteriol 171(7);3810-6. PMID: 2544557

Kowal95: Kowal AT, Werth MT, Manodori A, Cecchini G, Schroder I, Gunsalus RP, Johnson MK (1995). "Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase." Biochemistry 34(38);12284-93. PMID: 7547971

Lambden76: Lambden PR, Guest JR (1976). "Mutants of Escherichia coli K12 unable to use fumarate as an anaerobic electron acceptor." J Gen Microbiol 1976;97(2);145-60. PMID: 796407

Lancaster00: Lancaster CR, Kroger A (2000). "Succinate: quinone oxidoreductases: new insights from X-ray crystal structures." Biochim Biophys Acta 1459(2-3);422-31. PMID: 11004459

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Latour88: Latour DJ, Weiner JH (1988). "Regulation of in vitro expression of the Escherichia coli frd operon: alanine and Fnr represent positive and negative control elements." Nucleic Acids Res 16(14A);6339-52. PMID: 2456525

Leger01: Leger C, Heffron K, Pershad HR, Maklashina E, Luna-Chavez C, Cecchini G, Ackrell BA, Armstrong FA (2001). "Enzyme electrokinetics: energetics of succinate oxidation by fumarate reductase and succinate dehydrogenase." Biochemistry 40(37);11234-45. PMID: 11551223

Lemire82: Lemire BD, Robinson JJ, Weiner JH (1982). "Identification of membrane anchor polypeptides of Escherichia coli fumarate reductase." J Bacteriol 152(3);1126-31. PMID: 6754697

Lohmeier81: Lohmeier E, Hagen DS, Dickie P, Weiner JH (1981). "Cloning and expression of fumarate reductase gene of Escherichia coli." Can J Biochem 59(3);158-64. PMID: 7013950

LunaChavez00: Luna-Chavez C, Iverson TM, Rees DC, Cecchini G (2000). "Overexpression, purification, and crystallization of the membrane-bound fumarate reductase from Escherichia coli." Protein Expr Purif 2000;19(1);188-96. PMID: 10833406

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Other References Related to Gene Regulation

AboAmer04: Abo-Amer AE, Munn J, Jackson K, Aktas M, Golby P, Kelly DJ, Andrews SC (2004). "DNA interaction and phosphotransfer of the C4-dicarboxylate-responsive DcuS-DcuR two-component regulatory system from Escherichia coli." J Bacteriol 186(6);1879-89. PMID: 14996819

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ShalelLevanon05: Shalel-Levanon S, San KY, Bennett GN (2005). "Effect of ArcA and FNR on the expression of genes related to the oxygen regulation and the glycolysis pathway in Escherichia coli under microaerobic growth conditions." Biotechnol Bioeng 92(2):147-59. PMID: 15988767

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Zientz98: Zientz E, Bongaerts J, Unden G (1998). "Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system." J Bacteriol 1998;180(20);5421-5. PMID: 9765574


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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