, Volume 25, Issue 6, pp 603–606 | Cite as

Assemblierung des CuA-Zentrums in bakterieller Cytochrom-Oxidase

  • Fabia Canonica
  • Rudi Glockshuber
  • Hauke HenneckeEmail author
Wissenschaft Metallproteinbiogenese


The CuA cofactor in cytochrome oxidase of mitochondria and many aerobic prokaryotes is a di-copper metal center that catalyzes one-electron transfer from cytochrome c to the oxygen-reducing active site. How the two copper ions are brought together for assembly of CuA is reported here. A thioredoxin-like disulfide reductase and two dedicated metal-lochaperones, one for Cu2+ and one for Cu1+, cooperate in this process. Copper insertion into cytochrome oxidase proceeds by a previously unknown mechanism.


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  1. [1]
    Michel H, Behr J, Harrenga A et al. (1998) Cytochrome c oxidase: structure and spectroscopy. Annu Rev Biophys Biomol Struct 27:329–356CrossRefGoogle Scholar
  2. [2]
    Kroneck PMH (2018) Walking the seven lines: binuclear copper A in cytochrome c oxidase and nitrous oxide reductase. J Biol Inorg Chem 23:27–39CrossRefGoogle Scholar
  3. [3]
    Jett KA, Leary SC (2018) Building the CuA site of cytochrome c oxidase: a complicated, redox-dependent process driven by a surprisingly large complement of accessory proteins. J Biol Chem 293:4644–4652CrossRefGoogle Scholar
  4. [4]
    Abicht HK, Schärer MA, Quade N et al. (2014) How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation. J Biol Chem 289:32431–32444CrossRefGoogle Scholar
  5. [5]
    Canonica F, Klose D, Ledermann R et al. (2019) Structural basis and mechanism for metallochaperone-assisted assembly of the CuA center in cytochrome oxidase. Science Adv 5, doi: CrossRefGoogle Scholar
  6. [6]
    Serventi F, Youard ZA, Murset V et al. (2012) Copper starvation-inducible protein for cytochrome oxidase biogenesis in Bradyrhizobium japonicum. J Biol Chem 287:38812–38823CrossRefGoogle Scholar
  7. [7]
    Herrmann JM, Riemer J (2014) Three approaches to one problem: protein folding in the periplasm, the endoplasmic reticulum, and the intermembrane space. Antioxid Redox Signal 21:438–456CrossRefGoogle Scholar
  8. [8]
    Robinson NJ, Winge DR (2010) Copper metallochaperones. Annu Rev Biochem 79:537–562CrossRefGoogle Scholar
  9. [9]
    Banci L, Bertini I, Ciofi-Baffoni S et al. (2005) A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome oxidase. Proc Natl Acad Sci USA 102:3994–3999CrossRefGoogle Scholar
  10. [10]
    Thompson AK, Gray J, Liu A et al. (2012) The roles of Rhodobacter sphaeroides copper chaperones PCuAC and Sco (PrrC) in the assembly of the copper centers of the aa3-type and the cbb 3-type cytochrome c oxidases. Biochim Biophys Acta 1817:955–964CrossRefGoogle Scholar
  11. [11]
    Abriata LA, Banci L, Bertini I et al. (2008) Mechanism of CuA assembly. Nature Chem Biol 4:599–601CrossRefGoogle Scholar

Copyright information

© Springer-Verlag 2019

Authors and Affiliations

  • Fabia Canonica
    • 1
    • 2
  • Rudi Glockshuber
    • 1
    • 2
  • Hauke Hennecke
    • 2
    Email author
  1. 1.Institut für Molekularbiologie und BiophysikETH ZürichZürichSchweiz
  2. 2.Institut für MikrobiologieETH ZürichZürichSchweiz

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