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  • Description: succinate dehydrogenase(cytochrome b558 subunit)

Gene name sdhC
Essential no
Product succinate dehydrogenase (cytochrome b558 subunit)
Function TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 22 kDa, 9.831
Gene length, protein length 606 bp, 202 aa
Immediate neighbours yslB, sdhA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SdhC context.gif
This image was kindly provided by SubtiList

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
  • Localization: membrane protein PubMed

Database entries

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

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

Expression and regulation

  • Regulation: SdhC is less expressed under conditions of extreme iron starvation (FsrA) PubMed
  • Additional information:

Biological materials

  • Mutant: GP743 (sdhCA, cat), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks


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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] [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] [] (P p)

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