Show simple item record

dc.contributor.authorMaghool, S
dc.contributor.authorRyan, MT
dc.contributor.authorMaher, MJ
dc.date.accessioned2020-11-27T00:46:02Z
dc.date.available2020-11-27T00:46:02Z
dc.date.issued2020-10-01
dc.identifierpii: ijms21196983
dc.identifier.citationMaghool, 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.
dc.identifier.issn1422-0067
dc.identifier.urihttp://hdl.handle.net/11343/252584
dc.description.abstractComplex 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.
dc.languageEnglish
dc.publisherMDPI AG
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleWhat Role Does COA6 Play in Cytochrome C Oxidase Biogenesis: A Metallochaperone or Thiol Oxidoreductase, or Both?
dc.typeJournal Article
dc.identifier.doi10.3390/ijms21196983
melbourne.affiliation.departmentSchool of Chemistry
melbourne.source.titleInternational Journal of Molecular Sciences
melbourne.source.volume21
melbourne.source.issue19
melbourne.identifier.arcFT180100397
dc.rights.licenseCC BY
melbourne.elementsid1466587
melbourne.contributor.authorMaher, Megan
dc.identifier.eissn1422-0067
melbourne.identifier.fundernameidAustralian Research Council, FT180100397
melbourne.accessrightsOpen Access


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record