EPR spectroscopy of Escherichia coli cytochrome bo which lacks CuB

FEBS Letters

Hunter, Dominic J.B¹  Ingledew, W.John¹  Rich, Peter R²  Moody, A.John² 

[1] School of Biological and Medical Sciences, University of St. Andrews, St. Andrews, Fife, Scotland KY16 9AL, UK;Glynn Research Foundation, Glynn, Bodmin, Cornwall PL30 4AU, UK

关键词: Quinol oxidase;    Escherichia coli;    Copper depletion;    Ligand binding;    Electron paramagnetic resonance;    Cytochrome aa 3;    Cu(+) Cyt. bo;    cytochrome bo which contains CuB;    Cu(−) Cyt. bo;    cytochrome bo 3 lacking CuB;    Cu(+) membranes;    membranes derived from E. coli grown with a copper supplement;    containing only Cu(+) Cyt. bo;    Cu(−) membranes;    membranes derived from E. coli grown without a copper supplement and in the presence of a Cu(I) chelator;    containing a mixture of Cu(−) Cyt. bo and Cu(+) Cyt. bo);    BCA;    2;    2′-bicinchinonic acid (4;    4′-dicarboxy 2;    2′-biquinoline);    EPR;    electron paramagnetic resonance;    Ox;    unligated (oxidised) membranes;    CN;    cyanide-ligated membranes;    Su;    sulfide-ligated membranes;    Az;    azide-ligated membranes;    Flu;    fluoride-ligated membranes;    For;    formate-ligated membranes;   

DOI  :  10.1016/S0014-5793(97)00735-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The spectroscopic and ligand-binding properties of a copper-deficient cytochrome bo₃ , a member of the haem–copper superfamily of terminal oxidases, are reported and contrasted with those of the native enzyme. The enzyme lacks the copper atom (Cu_B) which is normally an integral part of the catalytic site. The consequences of loss of the Cu_B are the loss of antiferromagnetic coupling to the high-spin haem and an inability to form any of the integer-spin derivatives of the enzyme. Low-spin compounds of the normally high-spin haem are still formed with appropriate ligands, although these are modified.

【 授权许可】

Unknown