Integral caa3-Cytochrome c Oxidase from Thermus thermophilus: Purification and Crystallization

  • Orla SlatteryEmail author
  • Sabri Cherrak
  • Tewfik Soulimane
Part of the Methods in Molecular Biology book series (MIMB, volume 2039)


Cytochrome c oxidase is a respiratory enzyme catalyzing the energy-conserving reduction of molecular oxygen to water—a fundamental biological process of cell respiration. The first crystal structures of the type A cytochrome c oxidases, bovine heart and Paracoccus denitrificans cytochrome c oxidases, were published in 1995 and contributed immensely to the understanding of the enzyme’s mechanism of action. The senior author’s research focus was directed toward understanding the structure and function of the type B cytochrome c oxidases, ba3-oxidase and type A2 caa3-oxidase, both from the extreme thermophilic bacterium Thermus thermophilus. While the ba3-oxidase structure was published in 2000 and functional characterization is well-documented in the literature, we recently successfully solved the structure of the caa3-nature made enzyme-substrate complex. This chapter is dedicated to the purification and crystallization process of caa3-cytochrome c oxidase.

Key words

Cytochrome c oxidase caa3-Oxidase Chromatography Crystallization Bioenergetics Thermus thermophilus 


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Orla Slattery
    • 1
    • 2
    Email author
  • Sabri Cherrak
    • 1
    • 3
  • Tewfik Soulimane
    • 1
  1. 1.Department of Chemical Sciences, Bernal InstituteUniversity of LimerickLimerickIreland
  2. 2.Department of Biopharmaceutical and Medical ScienceGalway-Mayo Institute of TechnologyGalwayIreland
  3. 3.Department of BiologyUniversity Abou-Bekr BelkaidTlemcenAlgeria

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