Catalase Activity.

Bonnichsen, Roger; Chance, Britton; Theorell, Hugo; Linnasalmi, Annikki; Laukkanen, Pentti

doi:10.3891/acta.chem.scand.01-0685

Cited by 202 publications

(49 citation statements)

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“…DNA then binds this FS complex, and the catalytic cycle continues. This proposed mechanism is in contrast to the classical Iso-mechanisms (55), in which the enzyme converts back to its initial conformational state following release of substrate and prior to the start of a new catalytic cycle.…”

Section: A Special Role Of Adomet In the T4 Dam Methylationmentioning

confidence: 62%

“…Catalase is another enzyme with reaction rate characteristics similar to those of T4 Dam; e.g. it does not exhibit any tendency to saturate at high concentrations of substrate (55). If product release is the rate-limiting step of the reaction, then this type of behavior may be explained by the binding of substrate and release of product occurring in a concerted event.…”

Section: A Special Role Of Adomet In the T4 Dam Methylationmentioning

confidence: 99%

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Bacteriophage T4 Dam DNA-[N6-adenine]Methyltransferase

Evdokimov¹,

Zinoviev²,

Malygin³

et al. 2002

Journal of Biological Chemistry

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. After AdoHcy release, the enzyme remains in the F conformational form and is able to preferentially bind AdoMet (unlike form E, which randomly binds AdoMet and DNA), and the AdoMet-F binary complex then binds DNA to start another methylation cycle. We also propose an alternative pathway in which the release of AdoHcy is coordinated with the binding of AdoMet in a single concerted event, while T4 Dam remains in the isomerized form F. The resulting AdoMet-F binary complex then binds DNA, and another methylation reaction ensues. This route is preferred at high AdoMet concentrations.

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Section: A Special Role Of Adomet In the T4 Dam Methylationmentioning

confidence: 62%

Section: A Special Role Of Adomet In the T4 Dam Methylationmentioning

confidence: 99%

Bacteriophage T4 Dam DNA-[N6-adenine]Methyltransferase

Evdokimov¹,

Zinoviev²,

Malygin³

et al. 2002

Journal of Biological Chemistry

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“…The heme is well buried, 20 A below the molecular surface at a distance of only 23 A from the molecular center. This is particularly fascinating in light of the large turnover number of 100,000 per sec per active center, making catalase one of the few enzymes whose reaction rate approaches the limit set by substrate diffusion (51). The buried nature of the heme is, however, consistent with the unsuccessful attempts to replace the heme in catalase (19) and the pH of 2.4 required to completely extract the heme (52).…”

Section: Resultsmentioning

confidence: 99%

Structure and heme environment of beef liver catalase at 2.5 A resolution.

Reid¹,

Murthy²,

Sicignano³

et al. 1981

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

194

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Catalase (hydrogen peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) occurs in almost all aerobically respiring organisms and in part serves to protect cells from the toxic effects of hydrogen peroxide. The subcellular location of liver catalase is restricted to the peroxisomes, and the enzyme is probably incorporated into these organelles during their biogenesis (1). The properties of catalase have been reviewed by numerous authors including Deisseroth and Dounce (2) and Schonbaum and Chance (3). The overall reaction catalyzed by the enzyme can be written as ROOH + HQOH = QO + ROH + H20, [1] where R is H or an alkyl or acyl group and HQOH is a twoelectron donor in which Q is 0, C=O, or H(CH2)nCH (n = 1, 2, or 3). This reaction proceeds by two steps: (i) oxidation ofthe enzyme (E) by a peroxide E-H20 + ROOH = E-O + ROH + H20, [2] apocatalase I and (ii) oxidation of the substrate E-O + HQOH = E-H20 + QO.

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“…The rate of formation of compound I of HRP has been measured with methyl, ethyl (1), and hydroxymethyl (28) hydroperoxides and gave the respective rate constants 1.5, 3.6, and 0.5 all times lo6 M -I s-I which are much slower than for hydrogen peroxide. Bonnischsen et al (2) have measured the rate of hydrogen peroxide and horse blood catalase combination at 25 "C to be 3.5 x lo7 M -I s-l.…”

Section: Resultsmentioning

confidence: 99%

Horseradish Peroxidase. XVIII. The Arrhenius Activation Energy for the Formation of Compound I

Hewson¹,

Dunford²

1975

Can. J. Chem.

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The rate of formation of compound I from the reaction of native horseradish peroxidase with hydrogen peroxide was studied from 3.7–70.0 °C. The second-order rate constants were used to construct an Arrhenius plot from which the activation energy of this reaction was calculated to be 3.5 ± 1.0 kcal/mol. The irreversibility of the reaction at 25 °C was confirmed by comparing absolute absorbance changes as recorded by the stopped-flow apparatus with the known spectra of the native enzyme and compound I.

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Catalase Activity.

Cited by 202 publications

References 0 publications

Bacteriophage T4 Dam DNA-[N6-adenine]Methyltransferase

Bacteriophage T4 Dam DNA-[N6-adenine]Methyltransferase

Structure and heme environment of beef liver catalase at 2.5 A resolution.

Horseradish Peroxidase. XVIII. The Arrhenius Activation Energy for the Formation of Compound I

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