Description
Title: The Function of COA6 in the Copper Delivery Pathway from Mitochondria to Cytochrome c Oxidase
Abstract: Cytochrome c oxidase (CcO), the final enzyme in the mitochondrial respiratory chain, needs copper to remain stable and function. The CuB and CuA sites, which are two of the core subunits of CcO, are formed when copper is bound to COX1 and COX2, respectively. This mitochondrial copper delivery pathway is made up of several evolutionarily conserved proteins, which are necessary for the biogenesis of the two copper sites of CcO. The importance of comprehending copper delivery mechanisms to CcO from a biomedical standpoint has been highlighted by evidence that pathogenic mutations in some copper delivery pathway proteins, including SCO1, SCO2, and COA6, can result in fatal infantile human disorders. While two decades of research have shed more light on the biochemical functions of the SCO1 and SCO2 proteins, there is some disagreement regarding the role of COA6, the new member of this pathway. Following structural and functional studies, which demonstrated that COA6 is specifically needed for the biogenesis of the CuA site by acting as a disulfide reductase of SCO and COX2 proteins, it was discovered that initial genetic and biochemical studies had linked COA6 with copper delivery to COX2. It has also been suggested that it functions as a copper metallochaperone. Here, we provide a critical review of recent research on the molecular role of COA6 in CuA biogenesis.
Keywords: mitochondria; copper; cytochrome c oxidase; COA6; COX2; CuA site; metallochaperone;disulfide reductase
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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