Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.

Deisseroth, Albert; Dounce, Alexander L.

doi:10.1152/physrev.1970.50.3.319

Cited by 618 publications

(354 citation statements)

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“…It is of interest to note cytochrome bd is not the only example of a protein that contains a heme not reducible by dithionite. Nonreducibility of a high-spin heme b by dithionite also has been observed with many catalases in which the proximal ligand of heme b is tyrosine rather than histidine (43).…”

Section: Discussionmentioning

confidence: 73%

Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site

Belevich

Borisov

Zhang

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

119

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Section: Discussionmentioning

confidence: 73%

Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site

Belevich

Borisov

Zhang

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

119

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“…[7]. The enzyme can also be inactivated by complex formation within the protoheme-IX group, which is present in each subunit.…”

Section: Resultsmentioning

confidence: 99%

Activity and spectroscopic properties of bovine liver catalase in sodium bis(2‐ethylhexyl)sulfosuccinate/isooctane reverse micelles

Haber

Maśalakiewicz

Rodakiewicz-Nowak

et al. 1993

European Journal of Biochemistry

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Spectroscopic properties such as ultraviolet-visible spectroscopy, circular dichroism, steady-state fluorescence and the catalatic activity of bovine liver catalase (BLC) have been studied in reversemicelles microemulsions formed by sodium bis(2-ethy1hexyl)sulfosuccinate (AOT) in isooctane. Activity measurements were carried out with the highly water soluble hydrogen peroxide as substrate as a function of temperature and pH, at various concentrations of substrate, enzyme, AOTThe folding of catalase in reverse micelles is not drastically altered, although there are changes in the local surrounding of the prosthetic group. Kinetic measurements have been carried out under first-order conditions at low substrate concentration. They indicate that the measured substrate decomposition rate is limited by the exchange of substrate molecules between the substrate-filled and the enzyme-containing micelles. The specificity constant, k, = k,,,/K,, a$ related to water pool concentrations, k:",,, was, at all wo values, considerably lower than k, measured in buffer (k:). In contrast, overall values of k, in reverse micelles, kYiv, were always 2-4-times higher than k:. This apparent superactivity can, however, be ascribed to concentration effects.No 'bell-curve' to describe the w, dependence of catalase activity in reverse micelles was found, k or k, increasing monotonously up to wo = 50. Abbreviations. BLC, bovine liver catalase; AOT, sodium bis(2-ethylhexy1)sulfosuccinate; wnr ratio of molar concentration of water to the molar concentration of AOT (wl, = (H,O]/[AOT]); kh, k in buffer solution; k'", k in reverse micellar system; k,, the specificity constant (kcaJKM) ; k::kP, k, in reverse micelles related to water-pool concentrations; k&, k, i n reverse micelles related to the overall concentrations ; k,,, the substrate-exchange constant in the micellar system; vn, initial velocity.Enzyme. Bovine liver catalase (H,O,:H,O, oxidoreductase) (E. C. 1.11.1.6).Chemistry, Polish Academy of Sciences, 30 239 Cracow, Poland Native catalase is a tetrameric oxidoreductase with a relative molecular mass of 240000 [ 5 ] , catalyzing the conversion of water-soluble substrates such as hydrogen peroxide alone (in the catalatic activity) or together with low-chain donors such as alcohols, hydroxylamine or formic acid (in the peroxidatic activity) [6, 71. Catalase is a very fast enzyme (the catalytic constant, k,,, = 3.8 X lo7 s-', the Michaelis constant K,,, = 1.1 M and k,,,/K, = 3.5 X lo7 M-' s-' for the decomposition of H,O, at pH 7.0 [S]); this rate is thus comparable to the rate characterizing the dynamics of reversemicellar systems (the exchange rate constant, k,.., fir the intermicellar exchange of reactants is of the order 10h-108 M-' s-' [9, lo]). The effective rate constant measured for catalase in reverse micelles may therefore be dependent on the mass exchange between the micelles. If the enzymic reaction is faster than the exchange of substrate between the micelles, k,, will become the rate-limiting step. The observed rate consta...

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“…Hydrogen peroxide is metabolized by three different types of hydroperoxidases: catalase, peroxidase, and catalase-peroxidase. The typical catalases, which catalyze the dismutation of H202 to 02 and H20, have been isolated from animals, plants, and microorganisms (7,10). It is generally accepted that the major physiological role of the typical catalase is protection of the cells against the damaging effect of hydrogen peroxide (7).…”

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confidence: 99%

Physiological functions of hydroperoxidases in Rhodobacter capsulatus

1992

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Rhiodobacter capsulatus Jl has two hydroperoxidases: a catalase-peroxidase and a peroxidase. A mutant strain, AH18, that had no catalase-peroxidase was isolated. The growth rate under aerobic and photosynthetic conditions, respiration, superoxide dismutase and peroxidase activities, and pigment content of the mutant were similar to those of the wild type. AH18 was more susceptible to killing and to inhibition of nitrogenase by H202 but not by molecular oxygen. The incidences of spontaneous mutations were similar in both strains. Viable counts in aerobic but not anaerobic cultures of AH18 started to decline as soon as the cultures reached the stationary phase, and the rate of cell death was much higher in AH18 than in the wild type. It is inferred that the peroxidase provides protection against H202 in log-phase cells and that the catalase-peroxidase provides protection under the oxidative conditions that prevail in aging cultures. This protective function might be related to the dual activity of the latter as a catalase and a peroxidase or to its capacity to oxidize NADH, NADPH, and cytochrome c.Metabolic activation of molecular oxygen very often results in the production of hydrogen peroxide, which has been shown to be deleterious to most cellular components (12,29). The potential damage is especially significant in cells faced with stresses characteristic of special conditions. For example, photosynthetic organisms are challenged by the photodynamic reactions that enhance partial reduction of 02 (12); in nitrogen-free medium, diazotrophs are vulnerable because of the extreme lability to oxygen of the nitrogen fixation system (35); and elevated steady-state concentrations of toxic oxygen products play a significant role in aging of cells and tissues (15,16,35). Hydrogen peroxide is metabolized by three different types of hydroperoxidases: catalase, peroxidase, and catalase-peroxidase. The typical catalases, which catalyze the dismutation of H202 to 02 and H20, have been isolated from animals, plants, and microorganisms (7, 10). It is generally accepted that the major physiological role of the typical catalase is protection of the cells against the damaging effect of hydrogen peroxide (7). Peroxidase, which catalyzes oxidation of H202 by a large variety of substrates, also may function in detoxifying hydrogen peroxide as well as in various cellular activities of biosynthesis and degradation (12). The catalase-peroxidases, which were only recently classified as a distinct group of enzymes (19,33) tochrome c (unpublished data). These enzymes share biochemical and physicochemical properties with both catalases and peroxidases. Like the typical catalases they are tetramers, with a combined molecular mass of about 240,000 Da, and they have hydrophobic properties exhibited by their binding to phenyl-Sepharose. Unlike typical catalases and similar to peroxidases, the catalase-peroxidases are inactivated by ethanol-chloroform and are not inhibited by 3-amino-1,2,4-triazole, they have a sharp dependence of their activity...

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Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.

Cited by 618 publications

References 0 publications

Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site

Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site

Activity and spectroscopic properties of bovine liver catalase in sodium bis(2‐ethylhexyl)sulfosuccinate/isooctane reverse micelles

Physiological functions of hydroperoxidases in Rhodobacter capsulatus

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