Abstract:
:Bovine heart cytochrome c oxidase, depleted of polypeptide subunits by alkaline detergent treatment, was characterized with respect to metal content, optical spectral properties, and oxidase activity. Treatment with 1.0% Triton X-100 at pH 9.5 followed by anion-exchange chromatography caused removal of subunit III, subunit VII, and polypeptides a and b. The metal atom stoichiometries of the control and the polypeptide-depleted enzyme were in both cases 2.5Cu/2Fe/1Zn/1Mg with metal-to-protein ratios significantly greater in the latter. The treated enzyme exhibited a red shifted oxidized Soret maximum and bound carbon monoxide upon reduction. Activity was markedly decreased by the treatment but was restored to control levels by incubation with 0.3% Tween 80 at pH 6.0. Therefore, subunit III, subunit VII, polypeptide a, and polypeptide b do not contain Cu, Fe, Zn, or Mg and are not essential for reduction of O2 by ferrocytochrome c.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Yewey GL,Caughey WSdoi
10.1016/s0006-291x(87)80304-2subject
Has Abstractpub_date
1987-11-13 00:00:00pages
1520-6issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(87)80304-2journal_volume
148pub_type
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