Abstract
IN his first paper on cytochrome, Keilin1 reported in 1925 that the α-band of the ferrocytochrome at 604 mµ was shifted to 576 mµ by the action of potassium hydroxide on bee muscle and yeast cells. He ascribed this to a modification of his component a of cytochrome (later recognized as a mixture of cytochromes a and a3) into a ‘hæmochromogen A’. It appears remarkable that this shift of 28 mµ towards the blue, which is far greater than that accompanying the alkaline denaturation of other hæmoproteins except chlorocruorin, caused practically no comment. The action of strong alkali on cytochrome oxidase preparations has to my knowledge never been examined again for thirty-five years after Keilin's original observation.
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LEMBERG, R. Action of Alkali on Cytochrome Oxidase. Nature 193, 373–374 (1962). https://doi.org/10.1038/193373a0
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DOI: https://doi.org/10.1038/193373a0
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