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Catalases and Peroxidases

  • Chapter
Biochemistry of Dioxygen

Part of the book series: Biochemistry of the Elements ((BOTE,volume 4))

Abstract

Catalase is the enzyme that catalyzes the decomposition of hydrogen peroxide to water and dioxygen. The usual sources of catalase are bovine liver and bovine erythrocytes. The enzyme exists as a 250,000–dalton tetramer with one heme per monomer. The complete amino acid sequence of the bovine liver enzyme is known (Schroeder et al., 1982) as well as much of the sequence of the bovine erythrocyte catalase (Schroeder et al., 1982). The crystal structure of the beef liver enzyme has been determined (Reid et al., 1981; Murthy et al., 1981). The heme is buried in the enzyme accessible only by a 20–Å hydrophobic channel. There is a tyrosine group on one side of the heme and an asparagine and a histidine on the other. The negative charge of the tyrosine probably aids in the stability of the 4 + iron (Reid et al., 1981) intermediate to be discussed below.

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  1. University of California, Davis, Davis, California, USA

    Llyod L. Ingraham & Damon L. Meyer

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  1. Llyod L. Ingraham
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© 1985 Plenum Press, New York

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Ingraham, L.L., Meyer, D.L. (1985). Catalases and Peroxidases. In: Biochemistry of Dioxygen. Biochemistry of the Elements, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2475-1_6

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  • DOI: https://doi.org/10.1007/978-1-4613-2475-1_6

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