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Open AccessReview

Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations

1
Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET-UNR), Ocampo y Esmeralda, Rosario S2000EZP, Argentina
2
Plataforma de Biología Estructural y Metabolómica (PLABEM), Ocampo y Esmeralda, Rosario S2000EZP, Argentina
3
Area Biofísica, Departamento de Química Biológica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, Rosario S2002LRK, Argentina
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2019, 20(15), 3830; https://doi.org/10.3390/ijms20153830
Received: 23 June 2019 / Revised: 15 July 2019 / Accepted: 16 July 2019 / Published: 5 August 2019
Copper is an essential cofactor for aerobic respiration, since it is required as a redox cofactor in Cytochrome c Oxidase (COX). This ancient and highly conserved enzymatic complex from the family of heme-copper oxidase possesses two copper sites: CuA and CuB. Biosynthesis of the oxidase is a complex, stepwise process that requires a high number of assembly factors. In this review, we summarize the state-of-the-art in the assembly of COX, with special emphasis in the assembly of copper sites. Assembly of the CuA site is better understood, being at the same time highly variable among organisms. We also discuss the current challenges that prevent the full comprehension of the mechanisms of assembly and the pending issues in the field. View Full-Text
Keywords: copper site assembly; heme-copper oxidases; copper trafficking; metallochaperone copper site assembly; heme-copper oxidases; copper trafficking; metallochaperone
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MDPI and ACS Style

Llases, M.-E.; Morgada, M.N.; Vila, A.J. Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations. Int. J. Mol. Sci. 2019, 20, 3830.

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