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Poster

Mechanism of CuA Assembly in the Biogenesis of Cytochrome c Oxidase

Ms Banaja Dash, Prof. Dr Bernd Ludwig1
1 Group Leader of Molecular Genetics, Institute of Biochemistry

Abstract

Mechanism of CuA Assembly in the Biogenesis of
Cytochrome c Oxidase

Banaja Dash, Institute of Biochemistry, Molecular Genetics, Goethe University, Frankfurt am Main, Germany

Cytochrome c oxidase (COX) is a multi-subunit enzyme of the mitochondrial respiratory chain. The aa3 oxidases from bacteria are members of the same family, sharing many features of related enzymes, both functionally and structurally. Biogenesis of cytochrome c oxidase (COX) is a highly complex process involving >30 chaperones in eukaryotes; those required for the incorporation of the copper and heme cofactors are also conserved in bacteria. The proteins Cox17, Sco1/2, and Cox11 are necessary for copper insertion into CuA and CuB redox centers of COX in eukaryotes.

The proteins of the Sco family are discussed as potential cupper chaperones during the assembly of the CuA center in subunit II of the COX. The precise functions of the Sco proteins, however, remain unclear. The soil bacterium Paracoccus denitrificans contains homologous Sco proteins , designated as ScoA and ScoB. In this study we try to establish functional and structural roles for Sco proteins during COX biogenesis.


References

References:-

  1. Abajian, C. et al. (2006). “Crystal structure ofyeast sco1 with copper bound.” J. Biol. Inorg. Chem. 11: 459-466.
  2. Abriata, L. A. et al. (2008). “Mechanism of CuA assembly.” Nat. Chem. Biol. 4 (10): 599-601
  3. Banci, L. et al. (2006). “A hint for the function ofhuman Sco1 from different structures.” Proc. Natl.Acad. Sci. USA 103 (23): 8595-8600
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DOI®: 10.3288/contoo.paper.1700
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