A factor that stimulated iron-oxidase and cytochrome c oxidase of Thiobacillus ferrooxidans was purified from the bacterium. The stimulating factor was a copper-containing protein. The purified factor was homogeneous in disc-gel electrophoresis and showed absorption maxima at 278 nm, 400nm and 597 nm. The last absorption which corresponds to copper protein diminished after the addition of ferrous ions at pH 3.5. The yield of this factor from cells grown in medium supplemented with copper sulfate was twice that of cells grown in medium without copper sulfate.
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