Catalase activity at high concentration of hydrogen peroxide

doi:10.1016/0003-9861(55)90291-5

Archives of Biochemistry and Biophysics

Volume 57, Issue 2, August 1955, Pages 288-300

https://doi.org/10.1016/0003-9861(55)90291-5 Get rights and content

Abstract

1.
1. Using a two-mixer method, the over-all reaction of catalase was investigated from the kinetic point of view. The relationship between the rate of reaction and the substrate concentration fitted the Michaelis theory. The Michaelis constant was obtained as 1.1 M at 30 °.
2.
2. It is assumed that the inhibitions at acid and alkaline pH are caused by H⁺ and OH⁻ ions. These inhibitions seem to be reversible and non-competitive with the substrate.
3.
3. The inhibitions caused by cyanide, fluoride, and formate were competitive with the substrate. The Michaelis constant was calculated also from the mutual effects expected to occur between inhibitor and substrate and gave a mean value that was in good accord with the one above mentioned.
4.
4. Based on the data obtained, the two different mechanisms, which may be considered as the possible explanation of catalase reaction, are discussed. It is suggested that a compound ESS is formed in the reaction by another molecule of H₂O₂ reversibly to complex I.

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Citation Excerpt :
−0.7 V are less than twice their value in the absence of CAT. 2e-ORR catalyzed by CAT can be excluded due to the well-known ability of this enzyme to cause rapid disproportionation of H2O2 (reaction (1)) [6]. Currents higher than for diffusion-controlled 2e-ORR are only possible in the presence of an additional electroactive substance and/or a higher number of electrons involved in the Faradaic process.
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Archives of Biochemistry and Biophysics

Abstract

References (19)

J. Biochem. (Japan)

J. Am. Chem. Soc

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Cited by (116)

Peroxiredoxin-1 is an H<inf>2</inf>O<inf>2</inf> safe-guard antioxidant and signalling enzyme in M1 macrophages

A novel method to estimate biofilm activity based on enzymatic oxygen release from hydrogen peroxide decomposition

Study of catalase reversibility during multiple injections of H<inf>2</inf>O<inf>2</inf> using online measurement by FFT continuous cyclic voltammetry

Mediatorless electrocatalytic oxygen reduction with catalase on mercury–gold amalgam microelectrodes

NADH oxidase and alkyl hydroperoxide reductase subunit C (peroxiredoxin) from Amphibacillus xylanus form an oligomeric assembly

Heme Proteins in Lactic Acid Bacteria