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Escherichia coli K-12 substr. MG1655 Enzyme: 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

Gene-Reaction Schematic: ?

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
Curated 28-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


Subunit of succinate:quinone oxidoreductase: succinate:quinone oxidoreductase, FAD binding protein

Synonyms: DhsA, SdhA

Gene: sdhA Accession Numbers: EG10931 (EcoCyc), b0723, ECK0712

Locations: inner membrane, cytosol

Sequence Length: 588 AAs

Molecular Weight: 64.422 kD (from nucleotide sequence)

pI: 6.21

GO Terms:

Biological Process: GO:0006099 - tricarboxylic acid cycle Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA01a, Lin05]
GO:0009060 - aerobic respiration Inferred from experiment [Lin05, Park95]
GO:0055114 - oxidation-reduction process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Lin05]
GO:0022900 - electron transport chain Inferred by computational analysis [GOA01a]
Molecular Function: GO:0000104 - succinate dehydrogenase activity Inferred from experiment [Wood84]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Ruprecht09, Stenberg05, Yankovskaya03]
GO:0009055 - electron carrier activity Inferred from experiment [Lin05, Cecchini03]
GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment Inferred by computational analysis [GOA01a, Yankovskaya03, Brandsch89]
GO:0008177 - succinate dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016627 - oxidoreductase activity, acting on the CH-CH group of donors Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Stenberg05]
GO:0045282 - plasma membrane succinate dehydrogenase complex Inferred from experiment [Stenberg05]
GO:0005829 - cytosol
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon aerobic respiration
metabolism energy metabolism, carbon TCA cycle
metabolism energy production/transport electron donors

Unification Links: EcoliWiki:b0723 , Mint:MINT-6478272 , ModBase:P0AC41 , PR:PRO_000023918 , Pride:P0AC41 , Protein Model Portal:P0AC41 , RefSeq:NP_415251 , SMR:P0AC41 , String:511145.b0723 , UniProt:P0AC41

Relationship Links: InterPro:IN-FAMILY:IPR003952 , InterPro:IN-FAMILY:IPR003953 , InterPro:IN-FAMILY:IPR011281 , InterPro:IN-FAMILY:IPR013027 , InterPro:IN-FAMILY:IPR014006 , InterPro:IN-FAMILY:IPR015939 , InterPro:IN-FAMILY:IPR027477 , Panther:IN-FAMILY:PTHR11632:SF5 , 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:PF00890 , Pfam:IN-FAMILY:PF02910 , Prints:IN-FAMILY:PR00368 , Prosite:IN-FAMILY:PS00504

Summary:
This is one of two catalytic subunits in the four subunit succinate dehydrogenase (SQR) enzyme. This subunit contains the FAD cofactor [Brandsch89] and the substrate-binding site [Yankovskaya03].

Succinate, fumarate, citrate, and isocitrate appear to cause increased flavinylation of overproduced SdhA in cell extracts, indicating the existence of an activation mechanism involving TCA cycle intermediates [Brandsch89].

This protein has similarity to the FrdA subunit of fumarate reductase [Wood84]. A 2.2 Å crystal structure of L-aspartate oxidase suggests that an unusual tertiary structure is shared by L-aspartate oxidase, the SdhA subunit of succinate dehydrogenase, and the FrdA subunit of fumarate reductase [Mattevi99].

Citations: [Condon85]

Essentiality data for sdhA 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]

Subunit of succinate:quinone oxidoreductase: succinate:quinone oxidoreductase, iron-sulfur cluster binding protein

Synonyms: DhsB, SdhB

Gene: sdhB Accession Numbers: EG10932 (EcoCyc), b0724, ECK0713

Locations: cytosol, inner membrane

Sequence Length: 238 AAs

Molecular Weight: 26.77 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [Park95]
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:0005515 - protein binding Inferred from experiment [Rajagopala14, Ruprecht09, Stenberg05, Yankovskaya03]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01a, Cheng06]
GO:0051536 - iron-sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Morningstar85]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Werth92]
GO:0051538 - 3 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Johnson85]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Cammack86]
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]
Cellular Component: GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon aerobic respiration
metabolism energy metabolism, carbon TCA cycle
metabolism energy production/transport electron donors

Unification Links: DIP:DIP-10836N , EcoliWiki:b0724 , ModBase:P07014 , PR:PRO_000023919 , Pride:P07014 , Protein Model Portal:P07014 , RefSeq:NP_415252 , SMR:P07014 , String:511145.b0724 , UniProt:P07014

Relationship Links: InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR004489 , 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: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:PF13085 , Prosite:IN-FAMILY:PS00197 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51379

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

Summary:
This is one of two catalytic subunits of the four subunit succinate dehydrogenase (SQR) enzyme. This subunit contains three iron-sulfur clusters: a 2Fe-2S, a 4Fe-4S and a 3Fe-4S.

This subunit has 38% identity to the fumarate reductase iron-sulfur cluster subunit, FrdB [Darlison84a]. The iron-sulfur clusters of this subunit act as electron transfer redox centers, delivering electrons from the FAD cofactor in SdhA to the ubiquinone binding site within the membrane domain [Cecchini03].

sdhB is one of a network of genes believed to play a role in promoting the stress-induced mutagenesis (SIM) response of E. coli K-12 [Al12].

Citations: [Condon85]

Essentiality data for sdhB 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]

Subunit of succinate:quinone oxidoreductase: succinate:quinone oxidoreductase, membrane protein SdhC

Synonyms: DhsC, CybA, SdhC, large subunit of cytochrome b556, CybL

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

Locations: inner membrane

Sequence Length: 129 AAs

Molecular Weight: 14.299 kD (from nucleotide sequence)

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

Unification Links: EcoliWiki:b0721 , ModBase:P69054 , PR:PRO_000023920 , Protein Model Portal:P69054 , RefSeq:NP_415249 , 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

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]

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]

Subunit of succinate:quinone oxidoreductase: succinate:quinone oxidoreductase, membrane protein SdhC

Synonyms: DhsD, SdhD, CybS, small subunit of cytochrome b556

Gene: sdhD Accession Numbers: EG10934 (EcoCyc), b0722, ECK0711

Locations: inner membrane

Sequence Length: 115 AAs

Molecular Weight: 12.868 kD (from nucleotide sequence)

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:0009055 - electron carrier activity Inferred from experiment [Cecchini03]
GO:0020037 - heme binding Inferred from experiment Inferred by computational analysis [GOA01a, Vibat98]
GO:0000104 - succinate dehydrogenase activity Inferred by computational analysis [GOA01a]
GO:0008177 - succinate dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01]
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]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, 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

Unification Links: EcoliWiki:b0722 , ModBase:P0AC44 , PR:PRO_000023921 , Pride:P0AC44 , Protein Model Portal:P0AC44 , RefSeq:NP_415250 , SMR:P0AC44 , String:511145.b0722 , UniProt:P0AC44

Relationship Links: InterPro:IN-FAMILY:IPR000701 , InterPro:IN-FAMILY:IPR014312 , 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

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

Summary:
One of two membrane proteins in the four subunit enzyme. SdhC and SdhD are the large and small subunits of cytochrome b556, respectively [Nakamura96].

The b556 type heme bridges both membrane subunits [Maklashina99, Nakamura96]. Published reports disagree about whether mutation of SdhC-[His84] or SdhD-[His71] residues eliminate coordination of the heme b [Maklashina01, Vibat98]. Mutation of the residues coordinating the heme indicate that the heme helps stabilize the enzyme [Maklashina01]. SdhC-[His84] is involved in interaction with the quinone electron acceptor [Maklashina01]. SdhC-[His84] and SdhD-[His71] (with the associated heme b) are reported to be dispensable for assembly, while SdhC-[His30] is required for proper assembly of the membrane-bound enzyme [Vibat98].

Mutants lacking SdhC and SdhD show cytoplasmic succinate dehydrogenase activity using artificial electron acceptors, in contrast to wild-type membrane-associated succinate-ubiquinone oxidoreductase activity [Nakamura96, Neidhardt96].

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].

sdhD is one of a network of genes believed to play a role in promoting the stress-induced mutagenesis (SIM) response of E. coli K-12 [Al12].

Regulation has been described [Masse02, Takeda99, Cunningham98, Shen97, Park97, Xu95, Park95, Iuchi94, Silverman91, Iuchi89, Wilde86, Darlison84a, Shen97].

Essentiality data for sdhD 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]

References

Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554

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

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

Cammack86: Cammack R, Patil DS, Weiner JH (1986). "Evidence that centre 2 in Escherichia coli fumarate reductase is a [4Fe-4S]cluster." Biochim Biophys Acta 870(3);545-51. PMID: 3008846

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