SdhC

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  • Description: succinate dehydrogenase (cytochrome b558 subunit)

Gene name sdhC
Synonyms
Essential no
Product succinate dehydrogenase (cytochrome b558 subunit)
Function TCA cycle
Gene expression levels in SubtiExpress: sdhC
Interactions involving this protein in SubtInteract: SdhC
Metabolic function and regulation of this protein in SubtiPathways:
sdhC
MW, pI 22 kDa, 9.831
Gene length, protein length 606 bp, 202 aa
Immediate neighbours sdhA, yslB
Sequences Protein DNA DNA_with_flanks
Genetic context
SdhC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SdhC expression.png















Categories containing this gene/protein

carbon core metabolism, membrane proteins

This gene is a member of the following regulons

FsrA regulon

The gene

Basic information

  • Locus tag: BSU28450

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: cytochrome b558 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): Fe
  • Effectors of protein activity:
    • Inhibited by 2-(n-Heptyl)-4-hydroxy-quinoline N-oxide PubMed
    • Activated by Cytochrome b558 PubMed

Database entries

  • Structure: 1NEK (E. coli)
  • KEGG entry: [3]
  • E.C. number: 1.3.99.1

Additional information

  • This enzyme is a trimer membrane-bound PubMed PubMed
    • One subunit is bound to citochrome b558, and this subunit is the one bound to the cytosolic side of the membrane PubMed PubMed
    • Another subunit is the flavoprotein one, required for FAD usage PubMed PubMed
    • The other subunit has an iron-sulphur domain necessary for the catalytic activity PubMed PubMed
  • extensive information on the structure and enzymatic properties of succinate dehydrogenase can be found at Proteopedia

Expression and regulation

  • Regulation:
    • SdhC is less expressed under conditions of extreme iron starvation (FsrA) PubMed
    • part of the iron sparing response (FsrA) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Pedro M F Sousa, Marco A M Videira, Filipe A S Santos, Brian L Hood, Thomas P Conrads, Ana M P Melo
The bc:caa3 supercomplexes from the Gram positive bacterium Bacillus subtilis respiratory chain: a megacomplex organization?
Arch Biochem Biophys: 2013, 537(1);153-60
[PubMed:23880299] [WorldCat.org] [DOI] (I p)

Gregory T Smaldone, Olga Revelles, Ahmed Gaballa, Uwe Sauer, Haike Antelmann, John D Helmann
A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.
J Bacteriol: 2012, 194(10);2594-605
[PubMed:22389480] [WorldCat.org] [DOI] (I p)

Michael Baureder, Lars Hederstedt
Production, purification and detergent exchange of isotopically labeled Bacillussubtilis cytochrome b₅₅₈ (SdhC).
Protein Expr Purif: 2011, 80(1);97-101
[PubMed:21641999] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Ahmed Gaballa, Haike Antelmann, Claudio Aguilar, Sukhjit K Khakh, Kyung-Bok Song, Gregory T Smaldone, John D Helmann
The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.
Proc Natl Acad Sci U S A: 2008, 105(33);11927-32
[PubMed:18697947] [WorldCat.org] [DOI] (I p)

Victoria Yankovskaya, Rob Horsefield, Susanna Törnroth, César Luna-Chavez, Hideto Miyoshi, Christophe Léger, Bernadette Byrne, Gary Cecchini, So Iwata
Architecture of succinate dehydrogenase and reactive oxygen species generation.
Science: 2003, 299(5607);700-4
[PubMed:12560550] [WorldCat.org] [DOI] (I p)

M Matsson, D Tolstoy, R Aasa, L Hederstedt
The distal heme center in Bacillus subtilis succinate:quinone reductase is crucial for electron transfer to menaquinone.
Biochemistry: 2000, 39(29);8617-24
[PubMed:10913269] [WorldCat.org] [DOI] (P p)

C Hägerhäll, H Fridén, R Aasa, L Hederstedt
Transmembrane topology and axial ligands to hemes in the cytochrome b subunit of Bacillus subtilis succinate:menaquinone reductase.
Biochemistry: 1995, 34(35);11080-9
[PubMed:7669765] [WorldCat.org] [DOI] (P p)

C Hägerhäll, R Aasa, C von Wachenfeldt, L Hederstedt
Two hemes in Bacillus subtilis succinate:menaquinone oxidoreductase (complex II).
Biochemistry: 1992, 31(32);7411-21
[PubMed:1324713] [WorldCat.org] [DOI] (P p)

H Fridén, M R Cheesman, L Hederstedt, K K Andersson, A J Thomson
Low temperature EPR and MCD studies on cytochrome b-558 of the Bacillus subtilis succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron.
Biochim Biophys Acta: 1990, 1041(2);207-15
[PubMed:2176107] [WorldCat.org] [DOI] (P p)

L Melin, H Fridén, E Dehlin, L Rutberg, A von Gabain
The importance of the 5'-region in regulating the stability of sdh mRNA in Bacillus subtilis.
Mol Microbiol: 1990, 4(11);1881-9
[PubMed:1707123] [WorldCat.org] [DOI] (P p)

H Fridén, L Hederstedt
Role of His residues in Bacillus subtilis cytochrome b558 for haem binding and assembly of succinate: quinone oxidoreductase (complex II).
Mol Microbiol: 1990, 4(6);1045-56
[PubMed:2120540] [WorldCat.org] [DOI] (P p)

L Melin, L Rutberg, A von Gabain
Transcriptional and posttranscriptional control of the Bacillus subtilis succinate dehydrogenase operon.
J Bacteriol: 1989, 171(4);2110-5
[PubMed:2495271] [WorldCat.org] [DOI] (P p)

H Fridén, L Rutberg, K Magnusson, L Hederstedt
Genetic and biochemical characterization of Bacillus subtilis mutants defective in expression and function of cytochrome b-558.
Eur J Biochem: 1987, 168(3);695-701
[PubMed:3117551] [WorldCat.org] [DOI] (P p)

L Melin, K Magnusson, L Rutberg
Identification of the promoter of the Bacillus subtilis sdh operon.
J Bacteriol: 1987, 169(7);3232-6
[PubMed:3036777] [WorldCat.org] [DOI] (P p)

S T Cole, C Condon, B D Lemire, J H Weiner
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
[PubMed:3910107] [WorldCat.org] [DOI] (P p)

L Hederstedt, L Rutberg
Orientation of succinate dehydrogenase and cytochrome b558 in the Bacillus subtilis cytoplasmic membrane.
J Bacteriol: 1983, 153(1);57-65
[PubMed:6401289] [WorldCat.org] [DOI] (P p)

L Hederstedt, L Rutberg
Succinate dehydrogenase--a comparative review.
Microbiol Rev: 1981, 45(4);542-55
[PubMed:6799760] [WorldCat.org] [DOI] (P p)

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