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Gene Review

SDHD  -  succinate dehydrogenase complex, subunit D...

Bos taurus

Synonyms: CII-4, CII4, QPs3, cybS
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Disease relevance of SDHD

  • The smallest membrane-anchoring subunit (QPs3) of bovine heart succinate:ubiquinone reductase was overexpressed in Escherichia coli JM109 as a glutathione S-transferase fusion protein using the expression vector pGEX2T/QPs3 [1].

High impact information on SDHD

  • The recombinant QPs3 binds ubiquinone, causing a spectral blue shift [1].
  • Histidine residues at positions 46 and 60 are responsible for heme ligation because the H46N- or H60N-substituted QPs3 fail to restore cytochrome b560 upon addition of hemin chloride [1].
  • Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase [1].
  • Two amino acid residues, serine 33 and tyrosine 37, in the putative ubiquinone binding domain of QPs3 are involved in ubiquinone binding because the S33A- or Y37A-substituted recombinant QPs3s do not cause the spectral blue shift of ubiquinone [1].
  • The molecular mass of QPs3, deduced from the nucleotide sequence, is 10,989 Da [2].

Biological context of SDHD


Associations of SDHD with chemical compounds

  • The ubiquinone-binding domain in the proposed model of QPs3 is probably located at the end of transmembrane helix 1 toward the C-side of the mitochondrial inner membrane [2].
  • Although recombinant QPs3 contains little cytochrome b560 heme, the spectral characteristics of cytochrome b560 are reconstituted upon addition of hemin chloride [1].
  • CII-1 and CII-2 are the flavoprotein and iron-sulfur protein, respectively, of succinate dehydrogenase; CII-3 and CII-4 have not been functionally indentified [4].

Analytical, diagnostic and therapeutic context of SDHD

  • Upon titration of the recombinant protein with ubiquinone, a saturation behavior is observed, suggesting that the binding is specific and that recombinant QPs3 may be in the functionally active state [1].


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