Isolation and characterization of protoporphyrin IX from bacterial catalase.

Catalase has been isolated and crystallized from the bacterium, Micrococcus lysodeikticus, but the prosthetic group of the enzyme was identified only by indirect means (I). The method described by Herbert and Pinsent (1) for the isolation of catalase from bacteria employed 78 liters of starting material. This procedure could not be applied with equal success when the starting material consisted of only 1 liter of culture medium. The method described in the present communication is based on that of Herbert and Pinsent, but includes modifications which permit the isolation of relatively pure catalase from 1 liter of culture medium. Protoporphyrin IX has been characterized as the prosthetic group by isolation of the compound from the purified enzyme.