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What role does coa6 play in cytochrome c oxidase biogenesis: a metallochaperone or thiol oxidoreductase, or both?

journal contribution
posted on 02.12.2020, 02:19 by Shadi Maghool, MT Ryan, Megan Maher
© 2020, MDPI AG. All rights reserved. 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.

Funding

This research was funded by the Australian Research Council (DP140102746 and FT180100397 to MJM) and the National Health and Medical Research Council (GNT1165217 to MTR and MJM).

History

Publication Date

01/10/2020

Journal

International Journal of Molecular Sciences

Volume

21

Issue

19

Article Number

6983

Pagination

13p.

Publisher

MDPI

ISSN

1661-6596

Rights Statement

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