Comparative study of bacterial catalases

Varda Nadler, Iris Goldberg, Ayala Hochman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

78 Scopus citations

Abstract

Characterization of catalases from the photosynthetic bacteria Rhodopseudomonas capsulata and Rhodospirillum rubrum revealed that, while the latter is similar to the typical catalase of Micrococcus luteus, the former presents a number of strikingly different properties, which are shared by the enzyme of Escherichia coli. The catalase activity of R. rubrum, like that of the typical catalases, was pH-independent in the range 5.5-10, was inhibited by 3-amino-1,2,4-triazole, and was stable to treatment with the combination of organic solvents ethanol/chloroform. The enzymes of Rps. capsulata, and E. coli, on the other hand, showed a sharp maximum in their activity at pH 6-6.5, were not inhibited by 3-amino-1,2,4-triazole and were inactivated when treated with ethanol/chloroform mixture. Dialysis of Rps. capsulata and E. coli catalases against 2 mM H2O2 destroyed their activity with a half life of 20-30 min, while the typical catalases of R. rubrum and M. luteus were not affected by this treatment, even after one hour. The catalatic activities of the typical catalases, but not those of the Rps. capsulata and E. coli enzymes, were activated by temperature. Incubation of R. rubrum and M. luteus at 50°C for 5 min increased their activities by 188% and 155%, respectively. The catalases of Rps. capsulata and E. coli, unlike the typical catalases, are also peroxidases. We propose to consider the Rps. capsulata B10 and E. coli enzymes as prototypes of a new class of hydroperoxidases, designated catalase-peroxidase, which have intermediate properties between typical catalases and peroxidases. Preliminary experiments suggest that the enzymes of two other strains of Rps. capsulata, AD2 and BK5, and of Chromatium vinosum belong to this category, but Rps. sphaeroides R-26 and Forma sp. denitrificans have typical catalases.

Original languageEnglish
Pages (from-to)234-241
Number of pages8
JournalBiochimica et Biophysica Acta - General Subjects
Volume882
Issue number2
DOIs
StatePublished - 19 Jun 1986

Funding

FundersFunder number
United States-Israel Binational Science Foundation

    Keywords

    • Catalase
    • Peroxidase
    • Photosynthetic bacteria

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