Properties of the detergent solubilised cytochrome c oxidase (cytochrome cbb 3) purified from Pseudomonas stutzeri

FEBS Letters

Warne, Antony¹  Saraste, Matti¹  Urbani, Andrea¹  Gemeinhardt, Sabine¹ 

[1] European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhof str. 1, D-69117 Heidelberg, Germany

关键词: Cytochrome oxidase;    Membrane protein;    Crystallography;    Analytical ultracentrifugation;    Mass spectrometry;    Pseudomonas;    DM;    n-dodecyl-β-D-maltoside;    TMPD;    N;    N;    N′;    N′-tetramethyl-p-phenyldiamine;    TMBZ;    3;    3′;    5;    5′-tetramethylbenzidine;    TFA;    trifluoroacetic acid;    1 S;    1×10−13 s/rad−2;   

DOI  :  10.1016/S0014-5793(01)03006-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cytochrome cbb ₃ is a cytochrome c-oxidising isoenzyme that belongs to the superfamily of respiratory haem/copper oxidases. We have developed a purification method yielding large amounts of pure cbb ₃ complex from the soil bacterium Pseudomonas stutzeri. This cytochrome cbb ₃ complex consists of three subunits (ccoNOP) in a 1:1:1 stoichiometry and contains two b-type and three c-type haems. The protein complex behaves as a monomer with an overall molecular weight of 114.0±8.9 kDa and a s ⁰ _20,w value of 8.9±0.3 S as determined by analytical ultracentrifugation. Crystals diffracting to 5.0 Å resolution have been grown by the vapour diffusion sitting drop method to an average size of 0.1×0.1×0.3 mm. This is the first crystallisation report of a (cbb ₃)-type oxidase.

【 授权许可】

Unknown