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The catalase activity of ferrihaems.

ABSTRACT: 1. The variation of the specific stoicheiometric catalatic activity of proto- and deuteroferrihaem with total ferrihaem concentration has been studied at 25 degrees C over a wide range of pH. For deuteroferrihaem the results imply that only monomeric ferrihaem species contribute significantly to the catalatic activity. Protoferrihaem is more highly dimerized in solution and, in this system, contributions to the catalatic activity from both monomeric and dimeric ferrihaem species were observed. The ratio of the specific activity of protoferrihaem monomer to that of dimer varied from approximately 20 at pH7 to 5x10(4) at pH12.2. 2. The specific activity of protoferrihaem monomer closely resembles that of deuteroferrihaem monomer, both in magnitude and pH-dependence. In both cases the activity is inversely proportional to [H(+)]. In contrast, the activity of catalase is independent of pH in the range 5-10. At pH13 the activity of ferrihaem monomer becomes equal to the maximal activity of catalase. The results are in good agreement with those reported by Brown et al. (1970b) and provide support for the assumptions upon which this previous analysis relied. 3. Information from the literature concerning the catalatic activity and dimerization of the iron(III) complex of 4,4',4'',4'''-tetrasulphophthalocyanine (Waldmeier & Sigel, 1971; Sigel et al., 1971) have been re-analysed. The results imply that both the monomeric and dimeric complexes contribute to catalatic activity and these activities closely resemble those of the corresponding protoferrihaem species.

SUBMITTER: Jones P

PROVIDER: S-EPMC1165830 | biostudies-other | 1973 Oct

REPOSITORIES: biostudies-other

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Characterization of catalase from psychrotolerant Psychrobacter piscatorii T-3 exhibiting high catalase activity.

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| S-EPMC3291989 | biostudies-literature

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Catalase Protects Biofilm of Staphylococcus aureus against Daptomycin Activity.

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| S-EPMC8146090 | biostudies-literature

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An investigation of the relation between catalase <i>C262T</i> gene polymorphism and catalase enzyme activity in leukemia patients.

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