title: SPECTROSCOPY OF CATALASE.
abstract: Catalase is resistant to oxidizing agents; e.g., ferricyanide. It is also resistant to reducing agents; e.g., catalytically activated hydrogen, hydrosulfite, ferrotartrate, cysteine. The hemin group of the enzyme will combine with cyanide, sulfides, nitric oxide, fluoride. It will not combine with carbon monoxide. Catalase is therefore a ferric complex. The stability of the ferric iron in the enzyme toward reducing agents is not due to the structure of the porphyrin with which it is combined. This porphyrin is the protoporphyrin of the blood pigment. In combination with globin (methemoglobin) the ferric iron is readily reduced by the same reagents which have no effect on catalase. The stability of the ferric iron in the enzyme is therefore due to the protein component. It may be that the type of hematin-protein linkage in catalase is the reason for this phenomenon. The suggestion of Bersin (31), that sulfur may participate in this linkage, is interesting but, as yet, has no experimental basis. Hydrazine or pyridine and hydrosulfite convert catalase into hemochromogens containing ferrous iron. But in these hemochromogens the hematin is no longer attached to the protein. This has been replaced by the nitrogenous bases hydrazine and pyridine. Both hemochromogens combine reversibly with carbon monoxide. Photo-dissociation has only been demonstrated in the case of the pyridine hemochromogen. The positions of the absorption bands of catalase and its derivatives are listed in Table II. The main absorption band (Soret's band) of hemin complexes with nitrogenous substances (nitrogen bases, proteins) is situated at the border between the visible and the ultraviolet region of the spectrum. It has now been found that the spectrum of purified liver catalase has a well defined maximum of high extinction in this range, at 409 mmicro. This is further evidence for the hemin nature of the enzyme.
authors.affiliation: Courtauld Institute of Biochemistry, Middlesex Hospital Medical School, London, England, and the Laboratory of Physiological Chemistry, Yale University, New Haven).
authors.forename: K G
authors.initials: KG
authors.lastname: Stern