Abstract
We have studied the c.d. spectra of the 'Rieske' iron-sulphur protein isolated from the ubiquinol: cytochrome c reductase (bc1 complex) of bovine heart mitochondria. Both the oxidized and the reduced form of the 'Rieske' protein display a series of well-resolved c.d. features resembling those reported for the 'Rieske'-type iron-sulphur protein purified from the bacterium Thermus thermophilus [Fee, Findling, Yoshida, Hille, Tarr, Hearshen, Dunham, Day, Kent & Münck (1984) J. Biol, Chem. 259, 124-133]. In particular, the difference spectra, reduced minus oxidized, of both proteins have a distinctive negative band at 497 nm. The c.d. features characteristic of the isolated 'Rieske' protein were found in the dichroic spectra of the whole bc1 complex in the region between 450 and 520 nm. The reduction of the enzyme by ascorbate or ubiquinol is accompanied by the formation of a negative band at about 500 nm that corresponds, in all its c.d. properties, to the specific dichroic absorption of the reduced 'Rieske' iron-sulphur protein.
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