Abstract
A "double-alpha" c-type cytochrome, cytochrome c-555, 549, was isolated from the membrane fraction of an extreme thermophile, Thermus thermophilus HB8, and highly purified by chromatographies on DEAE-cellulose and Sephadex G-75 and by isoelectric focusing. The absorption maxima were at 554.8, 548.6, 522, and 417 nm in the reduced form, and at 528, 409, and 360 nm in the oxidized form. The double alpha-peak of this cytochrome was enhanced at liquid nitrogen temperature. The cytochrome contained one heme c group per protein molecule. The isoelectric point, midpoint redox potential and molecular weight were pH 4.0, +0.206 V and about 10,000, respectively. Cytochrome c-555, 549 is highly thermostable.
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