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Escherichia coli K-12 substr. MG1655 Polypeptide: succinate:quinone oxidoreductase, membrane protein SdhC



Gene: sdhC Accession Numbers: EG10933 (EcoCyc), b0721, ECK0710

Synonyms: cybL, cybA, dhsC, large subunit of cytochrome b556

Regulation Summary Diagram: ?

Component of: succinate:quinone oxidoreductase (extended summary available)

Summary:
SdhC is one of two membrane proteins in the four subunit succinate dehydrogenase (SQR) enzyme. SdhC and SdhD are the large and small subunits of cytochrome b556, respectively [Nakamura96]. The quinone binding (Qp) site resides in the interface between SdhB, SdhC and SdhD [Tran06].

The b556 type heme bridges both membrane subunits [Maklashina99, Nakamura96]. Mutation of key heme binding residues in SdhC and SdhD does not affect proper assembly or physiological function of the complex [Tran07].

Despite similar function, hydrophobicity, and protein size, the SdhC and SdhD subunits of succinate dehydrogenase do not share significant sequence identity with the corresponding membrane-binding subunits of fumarate reductase, FrdC and FrdD [Wood84].

Citations: [Neidhardt96]

Gene Citations: [Magnusson86, Cunningham98]

Locations: inner membrane

Map Position: [754,400 -> 754,789] (16.26 centisomes)
Length: 390 bp / 129 aa

Molecular Weight of Polypeptide: 14.299 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0002460 , CGSC:17902 , EchoBASE:EB0926 , EcoGene:EG10933 , EcoliWiki:b0721 , ModBase:P69054 , OU-Microarray:b0721 , PortEco:sdhC , PR:PRO_000023920 , Protein Model Portal:P69054 , RefSeq:NP_415249 , RegulonDB:EG10933 , SMR:P69054 , String:511145.b0721 , UniProt:P69054

Relationship Links: InterPro:IN-FAMILY:IPR000701 , InterPro:IN-FAMILY:IPR014314 , InterPro:IN-FAMILY:IPR014361 , InterPro:IN-FAMILY:IPR018495 , PDB:Structure:1NEK , PDB:Structure:1NEN , PDB:Structure:2ACZ , PDB:Structure:2AD0 , PDB:Structure:2WDQ , PDB:Structure:2WDR , PDB:Structure:2WDV , PDB:Structure:2WP9 , PDB:Structure:2WS3 , PDB:Structure:2WU2 , PDB:Structure:2WU5 , Pfam:IN-FAMILY:PF01127 , Prosite:IN-FAMILY:PS01000 , Prosite:IN-FAMILY:PS01001

Reactions known to consume the compound:

Not in pathways:
a ubiquinol-8 oxidoreductase + a b-type cytochrome → a ubiquinone-8 oxidoreductase + a reduced b-type cytochrome
a b-type cytochrome + a menaquinone oxidoreductase (demethylmenaquinol) → a reduced b-type cytochrome + a menaquinone oxidoreductase (demethylmenaquinone)
a b-type cytochrome + a menaquinone oxidoreductase (menaquinol-8) → a reduced b-type cytochrome + a menaquinone oxidoreductase (menaquinone-8)
a reduced b-type cytochrome + a b-type cytochromea b-type cytochrome + a reduced cytochrome o

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [Park95]
GO:0017004 - cytochrome complex assembly Inferred from experiment [Vibat98]
GO:0006099 - tricarboxylic acid cycle Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0008177 - succinate dehydrogenase (ubiquinone) activity Inferred by computational analysis Inferred from experiment [Yang98a, GOA01]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01a, Cecchini03]
GO:0020037 - heme binding Inferred from experiment [Vibat98]
GO:0048039 - ubiquinone binding Inferred from experiment [Yang98a]
GO:0000104 - succinate dehydrogenase activity Inferred by computational analysis [GOA01a]
GO:0016627 - oxidoreductase activity, acting on the CH-CH group of donors Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]
GO:0045281 - succinate dehydrogenase complex Inferred by computational analysis [GOA01a]

MultiFun Terms: cell structure membrane
metabolism biosynthesis of macromolecules (cellular constituents) large molecule carriers cytochromes
metabolism energy metabolism, carbon aerobic respiration
metabolism energy metabolism, carbon TCA cycle
metabolism energy production/transport electron donors

Essentiality data for sdhC 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:
Revised 15-Apr-2008 by Nolan L , Macquarie University
Last-Curated ? 28-Apr-2008 by Nolan L , Macquarie University


Subunit of: succinate:quinone oxidoreductase

Synonyms: SQR, complex II, succinate-ubiquinone oxidoreductase, SdhCDAB

Subunit composition of succinate:quinone oxidoreductase = [SdhA][SdhB][SdhC][SdhD]
         succinate:quinone oxidoreductase, FAD binding protein = SdhA (summary available)
         succinate:quinone oxidoreductase, iron-sulfur cluster binding protein = SdhB (summary available)
         succinate:quinone oxidoreductase, membrane protein SdhC = SdhC (summary available)
         succinate:quinone oxidoreductase, membrane protein SdhC = SdhD (extended summary available)

Summary:
Succinate dehydrogenase or succinate:quinone oxidoreductase (SQR) catalyses the oxidation of succinate to fumarate concomitant with the reduction of ubiquinone to ubiquinol. SQR plays an important role in cellular metabolism and directly connects the the TCA cycle with the respiratory electron transport chain. As part of the TCA cycle succinate is oxidized to fumarate by SQR and electrons are transferred to the membrane quinone pool for entry into the electron transport chain.

E.coli SQR (SdhCDAB) is a membrane bound heterotetramer [Kita89]. Subunits SdhA and SdhB are hydrophilic and attached to the cytoplasmic surface of the plasma membrane via interactions with the two hydrophobic integral membrane subunits, SdhC and SdhD. SdhA contains the FAD cofactor [Brandsch89] and the dicarboxylic acid binding site [Yankovskaya03]. Electrons from the oxidation of succinate are transferred through the iron-sulphur protein, SdhB, to a quinone binding site located at the interface of the SdhB, SdhC and SdhD subunits [Tran06]. The SdhC and SdhD subunits each contain three transmembrane helices and anchor the complex to the membrane. A single heme b556 cofactor bridges the SdhC and SdhD subunits [Nakamura96]. Crystal structures and electrophoretic and spectrometric analyses indicate that E. coli SQH is organised into a trimeric supercomplex [Yankovskaya03, Sousa11].

SQR is structurally and functionally homologous to fumarate reductase or menaquinol:fumarate reductase (QFR) which catalyses the reduction of fumarate to succinate under anaerobic conditions. The functions of SQR and QFR 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 dehyrdogenase supports the growth of an frd mutant [Maklashina98]. The SQR redox centres are arranged in a manner that aids the prevention of reactive oxygen species, providing a likely reason for the expression of SQR during aerobic respiration rather than QFR (which promotes high levels of oxygen radicals) [Yankovskaya03].

The sdhCDAB operon is expressed from a single promoter located upstream of sdhC [Park95, Park97]. sdhCDAB is optimally expressed during aerobic cell growth. Expression of the operon decreases substantially when cells are shifted to anaerobic growth [Shen97]. Negative control occurs by a repression mechanism due to binding of ArcA at the sdhC promoter [Iuchi89, Iuchi94]. The sdh operon is also catabolite controlled, gene expression varies when cells are grown aerobically with different compounds [Park95].

Crystal structures of E. coli SQR with an empty quinone binding site and with the quinone binding site occupied by various inhibitors have been determined [Yankovskaya03, Ruprecht09, Horsefield06].

Reviews: [Cecchini02, Gunsalus94, Hagerhall96].
Comment: [Hederstedt03]

Citations: [Ohnishi87, Condon85, Creaghan78, Spencer74, ZhdanPushkina86, Wood84, Darlison84a, Pershad99, Hederstedt81, Wilde86, Nihei01, Vibat98, Maklashina01, Yang98a, Yang97, Tornroth02, Barker00, Maklashina99, Tomasiak08, Shimizu08]

Locations: inner membrane

Relationship Links: PDB:Structure:1NEN , PDB:Structure:2ACZ , PDB:Structure:2WDQ , PDB:Structure:2WDR , PDB:Structure:2WDV

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [Hirsch63, Park95]
GO:0006099 - tricarboxylic acid cycle Inferred by computational analysis [GOA00, GOA01a]
Molecular Function: GO:0000104 - succinate dehydrogenase activity Inferred by computational analysis Inferred from experiment [Hirsch63, GOA01, Kita89]
GO:0009055 - electron carrier activity Inferred by computational analysis Inferred from experiment [Cheng06, GOA01a]
Cellular Component: GO:0031224 - intrinsic component of membrane Inferred from experiment Inferred by computational analysis [GOA00, Kita89]
GO:0045257 - succinate dehydrogenase complex (ubiquinone) Inferred from experiment Inferred by computational analysis [GOA01, Kita89]
GO:0005886 - plasma membrane [Kita89]

Credits:
Revised 15-Apr-2008 by Nolan L , Macquarie University
Last-Curated ? 14-Mar-2010 by Mackie A , Macquarie University


Enzymatic reaction of: succinate:quinone oxidoreductase

Synonyms: SQR, succinate-ubiquinone oxidoreductase, succinate-Q reductase, succinate dehydrogenase

EC Number: 1.3.5.1

In Pathways: superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , superpathway of glyoxylate bypass and TCA , TCA cycle I (prokaryotic) , succinate to cytochrome bo oxidase electron transfer , succinate to cytochrome bd oxidase electron transfer

Citations: [Hederstedt81, Ohnishi87]

Cofactors or Prosthetic Groups: a [4Fe-4S] iron-sulfur cluster , protoheme IX [Kita78], [2Fe-2S] iron-sulfur cluster , FAD [Brandsch89, Kita89], [3Fe-4S] iron-sulfur cluster

Inhibitors (Competitive): a 2-alkyl-dinitrophenol derivative , menaquinone-1 , malonate [Maklashina99] , pentachlorophenol [Maklashina99]

Inhibitors (Other): carboxin [Maklashina99]

Primary Physiological Regulators of Enzyme Activity: malonate


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 27 -> 52
[UniProt10]
UniProt: Helical;
Transmembrane-Region 69 -> 89
[UniProt10]
UniProt: Helical;
Metal-Binding-Site 84
[UniProt10]
UniProt: Iron (heme axial ligand); shared with second transmembrane subunit;
Transmembrane-Region 109 -> 129
[UniProt10]
UniProt: Helical;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0721 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10933; confirmed by SwissProt match.


References

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Barker00: Barker HC, Kinsella N, Jaspe A, Friedrich T, O'Connor CD (2000). "Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide." Mol Microbiol 35(6);1518-29. PMID: 10760151

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

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

Cecchini03: Cecchini G, Maklashina E, Yankovskaya V, Iverson TM, Iwata S (2003). "Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases." FEBS Lett 545(1);31-8. PMID: 12788489

Cheng06: Cheng VW, Ma E, Zhao Z, Rothery RA, Weiner JH (2006). "The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow." J Biol Chem 281(37);27662-8. PMID: 16864590

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Creaghan78: Creaghan IT, Guest JR (1978). "Succinate dehydrogenase-dependent nutritional requirement for succinate in mutants of Escherichia coli K12." J Gen Microbiol 107(1);1-13. PMID: 366070

Cunningham98: Cunningham L, Guest JR (1998). "Transcription and transcript processing in the sdhCDAB-sucABCD operon of Escherichia coli." Microbiology 144 ( Pt 8);2113-23. PMID: 9720032

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

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

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

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

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

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Gunsalus94: Gunsalus RP, Park SJ (1994). "Aerobic-anaerobic gene regulation in Escherichia coli: control by the ArcAB and Fnr regulons." Res Microbiol 145(5-6);437-50. PMID: 7855430

Hagerhall96: Hagerhall C, Hederstedt L (1996). "A structural model for the membrane-integral domain of succinate: quinone oxidoreductases." FEBS Lett 389(1);25-31. PMID: 8682198

Hederstedt03: Hederstedt L (2003). "Structural biology. Complex II is complex too." Science 299(5607);671-2. PMID: 12560540

Hederstedt81: Hederstedt L, Rutberg L (1981). "Succinate dehydrogenase--a comparative review." Microbiol Rev 1981;45(4);542-55. PMID: 6799760

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

Horsefield06: Horsefield R, Yankovskaya V, Sexton G, Whittingham W, Shiomi K, Omura S, Byrne B, Cecchini G, Iwata S (2006). "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 281(11);7309-16. PMID: 16407191

Iuchi89: Iuchi S, Cameron DC, Lin EC (1989). "A second global regulator gene (arcB) mediating repression of enzymes in aerobic pathways of Escherichia coli." J Bacteriol 171(2);868-73. PMID: 2644240

Iuchi94: Iuchi S, Aristarkhov A, Dong JM, Taylor JS, Lin EC (1994). "Effects of nitrate respiration on expression of the Arc-controlled operons encoding succinate dehydrogenase and flavin-linked L-lactate dehydrogenase." J Bacteriol 1994;176(6);1695-701. PMID: 8132465

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

Kita78: Kita K, Yamato I, Anraku Y (1978). "Purification and properties of cytochrome b556 in the respiratory chain of aerobically grown Escherichia coli K12." J Biol Chem 253(24);8910-5. PMID: 363711

Kita89: Kita K, Vibat CR, Meinhardt S, Guest JR, Gennis RB (1989). "One-step purification from Escherichia coli of complex II (succinate: ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556." J Biol Chem 264(5);2672-7. PMID: 2644269

Magnusson86: Magnusson K, Philips MK, Guest JR, Rutberg L (1986). "Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex." J Bacteriol 1986;166(3);1067-71. PMID: 3086287

Maklashina01: Maklashina E, Rothery RA, Weiner JH, Cecchini G (2001). "Retention of heme in axial ligand mutants of succinate-ubiquinone xxidoreductase (complex II) from Escherichia coli." J Biol Chem 276(22);18968-76. PMID: 11259408

Maklashina98: Maklashina E, Berthold DA, Cecchini G (1998). "Anaerobic expression of Escherichia coli succinate dehydrogenase: functional replacement of fumarate reductase in the respiratory chain during anaerobic growth." J Bacteriol 180(22);5989-96. PMID: 9811659

Maklashina99: Maklashina E, Cecchini G (1999). "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(2);223-32. PMID: 10486141

Nakamura96: Nakamura K, Yamaki M, Sarada M, Nakayama S, Vibat CR, Gennis RB, Nakayashiki T, Inokuchi H, Kojima S, Kita K (1996). "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 271(1);521-7. PMID: 8550613

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

Nihei01: Nihei C, Nakayashiki T, Nakamura K, Inokuchi H, Gennis RB, Kojima S, Kita K (2001). "Abortive assembly of succinate-ubiquinone reductase (complex II) in a ferrochelatase-deficient mutant of Escherichia coli." Mol Genet Genomics 265(3);394-404. PMID: 11405622

Ohnishi87: Ohnishi T "Structure of the succinate-ubiquinone oxidoreductase (complex II)." Current Topics in Bioenergetics 1987;15:37-65.

Park95: Park SJ, Tseng CP, Gunsalus RP (1995). "Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr." Mol Microbiol 15(3);473-82. PMID: 7783618

Park97: Park SJ, Chao G, Gunsalus RP (1997). "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 179(13);4138-42. PMID: 9209026

Pershad99: Pershad HR, Hirst J, Cochran B, Ackrell BA, Armstrong FA (1999). "Voltammetric studies of bidirectional catalytic electron transport in Escherichia coli succinate dehydrogenase: comparison with the enzyme from beef heart mitochondria." Biochim Biophys Acta 1412(3);262-72. PMID: 10482788

Ruprecht09: Ruprecht J, Yankovskaya V, Maklashina E, Iwata S, Cecchini G (2009). "Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site." J Biol Chem 284(43);29836-46. PMID: 19710024

Shen97: Shen J, Gunsalus RP (1997). "Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB) gene expression in Escherichia coli." Mol Microbiol 26(2);223-36. PMID: 9383149

Shimizu08: Shimizu H, Nihei C, Inaoka DK, Mogi T, Kita K, Harada S (2008). "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 64(Pt 9);858-62. PMID: 18765923

Sousa11: Sousa PM, Silva ST, Hood BL, Charro N, Carita JN, Vaz F, Penque D, Conrads TP, Melo AM (2011). "Supramolecular organizations in the aerobic respiratory chain of Escherichia coli." Biochimie 93(3);418-25. PMID: 21040753

Spencer74: Spencer ME, Guest JR (1974). "Proteins of the inner membrane of Escherichia coli: identification of succinate dehydrogenase by polyacrylamide gel electrophoresis with sdh amber mutants." J Bacteriol 117(3);947-53. PMID: 4591960

Tomasiak08: Tomasiak TM, Maklashina E, Cecchini G, Iverson TM (2008). "A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II." J Biol Chem 283(22);15460-8. PMID: 18385138

Tornroth02: Tornroth S, Yankovskaya V, Cecchini G, Iwata S (2002). "Purification, crystallisation and preliminary crystallographic studies of succinate:ubiquinone oxidoreductase from Escherichia coli." Biochim Biophys Acta 1553(1-2);171-6. PMID: 11803025

Tran06: Tran QM, Rothery RA, Maklashina E, Cecchini G, Weiner JH (2006). "The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b." J Biol Chem 281(43);32310-7. PMID: 16950775

Tran07: Tran QM, Rothery RA, Maklashina E, Cecchini G, Weiner JH (2007). "Escherichia coli succinate dehydrogenase variant lacking the heme b." Proc Natl Acad Sci U S A 104(46);18007-12. PMID: 17989224

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Vibat98: Vibat CR, Cecchini G, Nakamura K, Kita K, Gennis RB (1998). "Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli." Biochemistry 37(12);4148-59. PMID: 9521736

Wilde86: Wilde RJ, Guest JR (1986). "Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12." J Gen Microbiol 1986;132 ( Pt 12);3239-51. PMID: 3309132

Wood84: Wood D, Darlison MG, Wilde RJ, Guest JR (1984). "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli." Biochem J 1984;222(2);519-34. PMID: 6383359

Yang97: Yang X, Yu L, Yu CA (1997). "Resolution and reconstitution of succinate-ubiquinone reductase from Escherichia coli." J Biol Chem 272(15);9683-9. PMID: 9092498

Yang98a: Yang X, Yu L, He D, Yu CA (1998). "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 273(48);31916-23. PMID: 9822661

Yankovskaya03: Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S (2003). "Architecture of succinate dehydrogenase and reactive oxygen species generation." Science 299(5607);700-4. PMID: 12560550

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

ZhdanPushkina86: Zhdan-Pushkina SM, Verbitskaia NB, Kondrat'eva LD (1986). "[Succinate dehydrogenase activity of Escherichia coli cells after heat stress and during the reparative process]." Mikrobiologiia 55(3);357-61. PMID: 3528770

Other References Related to Gene Regulation

Desnoyers12: Desnoyers G, Masse E (2012). "Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq." Genes Dev 26(7);726-39. PMID: 22474262

Geissmann04: Geissmann TA, Touati D (2004). "Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator." EMBO J 23(2);396-405. PMID: 14739933

Iuchi88: Iuchi S, Lin EC (1988). "arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways." Proc Natl Acad Sci U S A 1988;85(6);1888-92. PMID: 2964639

Kumar11: Kumar R, Shimizu K (2011). "Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures." Microb Cell Fact 10;3. PMID: 21272324

Lynch96: Lynch AS, Lin EC (1996). "Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: characterization of DNA binding at target promoters." J Bacteriol 1996;178(21);6238-49. PMID: 8892825

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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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