What Role Does COA6 Play in Cytochrome C Oxidase Biogenesis: A Metallochaperone or Thiol Oxidoreductase, or Both?
AuthorMaghool, S; Ryan, MT; Maher, MJ
Source TitleInternational Journal of Molecular Sciences
University of Melbourne Author/sMaher, Megan
AffiliationSchool of Chemistry
Document TypeJournal Article
CitationsMaghool, S., Ryan, M. T. & Maher, M. J. (2020). What Role Does COA6 Play in Cytochrome C Oxidase Biogenesis: A Metallochaperone or Thiol Oxidoreductase, or Both?. International Journal of Molecular Sciences, 21 (19), https://doi.org/10.3390/ijms21196983.
Access StatusOpen Access
ARC Grant codeARC/FT180100397
Complex IV (cytochrome c oxidase; COX) is the terminal complex of the mitochondrial electron transport chain. Copper is essential for COX assembly, activity, and stability, and is incorporated into the dinuclear CuA and mononuclear CuB sites. Multiple assembly factors play roles in the biogenesis of these sites within COX and the failure of this intricate process, such as through mutations to these factors, disrupts COX assembly and activity. Various studies over the last ten years have revealed that the assembly factor COA6, a small intermembrane space-located protein with a twin CX9C motif, plays a role in the biogenesis of the CuA site. However, how COA6 and its copper binding properties contribute to the assembly of this site has been a controversial area of research. In this review, we summarize our current understanding of the molecular mechanisms by which COA6 participates in COX biogenesis.
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