Literature DB >> 4720713

The characteristics of the "peroxidatic" reaction of catalase in ethanol oxidation.

N Oshino, R Oshino, B Chance.   

Abstract

Ethanol oxidation by rat liver catalase (the ;peroxidatic' reaction) was studied quantitatively with respect to the rate of H(2)O(2) generation, catalase haem concentration, ethanol concentration and the steady-state concentration of the catalase-H(2)O(2) intermediate (Compound I). At a low ratio of H(2)O(2)-generation rate to catalase haem concentration, the rate of ethanol oxidation was independent of the catalase haem concentration. The magnitude of the inhibition of ethanol oxidation by cyanide was not paralleled by the formation of the catalase-cyanide complex and was altered greatly by varying either the ethanol concentration or the ratio of the rate of H(2)O(2) generation to catalase haem concentration. The ethanol concentration producing a half-maximal activity was also dependent on the ratio of the H(2)O(2)-generation rate to catalase haem concentration. These phenomena are explained by changes in the proportion of the ;catalatic' and ;peroxidatic' reactions in the overall H(2)O(2)-decomposition reaction. There was a correlation between the proportion of the ;peroxidatic' reaction in the overall catalase reaction and the steady-state concentration of the catalase-H(2)O(2) intermediate. Regardless of the concentration of ethanol and the rate of H(2)O(2) generation, a half-saturation of the steady state of the catalase-H(2)O(2) intermediate indicated that about 45% of the H(2)O(2) was being utilized by the ethanol-oxidation reaction. The results reported show that the experimental results in the study on the ;microsomal ethanol-oxidation system' may be reinterpreted and the catalase ;peroxidatic' reaction provides a quantitative explanation for the activity hitherto attributed to the ;microsomal ethanol-oxidation system'.

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Year:  1973        PMID: 4720713      PMCID: PMC1177502          DOI: 10.1042/bj1310555

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  37 in total

1.  METHANOL METABOLISM IN THE RAT.

Authors:  T R TEPHLY; R E PARKS; G J MANNERING
Journal:  J Pharmacol Exp Ther       Date:  1964-03       Impact factor: 4.030

2.  METHANOL METABOLISM IN THE ISOLATED PERFUSED RAT LIVER.

Authors:  D R VANHARKEN; T R TEPHLY; G J MANNERING
Journal:  J Pharmacol Exp Ther       Date:  1965-07       Impact factor: 4.030

3.  Primary compounds of catalase and peroxidase.

Authors:  A S Brill; R J Williams
Journal:  Biochem J       Date:  1961-02       Impact factor: 3.857

4.  The role of H 2 O 2 generation in perfused rat liver and the reaction of catalase compound I and hydrogen donors.

Authors:  N Oshino; B Chance; H Sies; T Bücher
Journal:  Arch Biochem Biophys       Date:  1973-01       Impact factor: 4.013

5.  Alcohol mixed function. Oxidase activity of mammalian liver microsomes.

Authors:  W H Orme-Johnson; D M Ziegler
Journal:  Biochem Biophys Res Commun       Date:  1965-10-08       Impact factor: 3.575

6.  Hepatic microsomal ethanol oxidizing system (MEOS): differentiation from alcohol dehydrogenase and NADPH oxidase.

Authors:  C S Lieber; E Rubin; L M DeCarli
Journal:  Biochem Biophys Res Commun       Date:  1970-08-24       Impact factor: 3.575

7.  Ethanol oxidation in the microsomal fraction of rat liver.

Authors:  M K Roach; W N Reese; P J Creaven
Journal:  Biochem Biophys Res Commun       Date:  1969-08-15       Impact factor: 3.575

8.  Analysis of the catalase--hydrogen peroxide intermediate in coupled oxidations.

Authors:  B Chance; N Oshino
Journal:  Biochem J       Date:  1973-03       Impact factor: 3.857

9.  Ethanol increases hepatic smooth endoplasmic reticulum and drug-metabolizing enzymes.

Authors:  E Rubin; F Hutterer; C S Lieber
Journal:  Science       Date:  1968-03-29       Impact factor: 47.728

10.  Ethanol oxidation by hepatic microsomes: adaptive increase after ethanol feeding.

Authors:  C S Lieber; L M DeCarli
Journal:  Science       Date:  1968-11-22       Impact factor: 47.728

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  30 in total

1.  Oxidation of methanol, formaldehyde and formate by catalase purified from methanol-grown Hansenula polymorpha.

Authors:  J P van Dijken; R Otto; W Harder
Journal:  Arch Microbiol       Date:  1975-12-31       Impact factor: 2.552

2.  The properties of hydrogen peroxide production under hyperoxic and hypoxic conditions of perfused rat liver.

Authors:  N Oshino; D Jamieson; B Chance
Journal:  Biochem J       Date:  1975-01       Impact factor: 3.857

3.  Optical measurement of the catalase-hydrogen peroxide intermediate (Compound I) in the liver of anaesthetized rats and its implication to hydrogen peroxide production in situ.

Authors:  N Oshino; D Jamieson; T Sugano; B Chance
Journal:  Biochem J       Date:  1975-01       Impact factor: 3.857

4.  Glyoxylate decarboxylation during photorespiration.

Authors:  B Grodzinski
Journal:  Planta       Date:  1978-01       Impact factor: 4.116

5.  Analysis of the catalase--hydrogen peroxide intermediate in coupled oxidations.

Authors:  B Chance; N Oshino
Journal:  Biochem J       Date:  1973-03       Impact factor: 3.857

6.  Biochemical and developmental characterization of multiple forms of catalase in tobacco leaves.

Authors:  E A Havir; N A McHale
Journal:  Plant Physiol       Date:  1987-06       Impact factor: 8.340

7.  Cytochemical studies on the localization of methanol oxidase and other oxidases in peroxisomes of methanol-grown Hansenula polymorpha.

Authors:  M Veenhuis; J P van Dijken; W Harder
Journal:  Arch Microbiol       Date:  1976-12-01       Impact factor: 2.552

8.  Properties of glutathione release observed during reduction of organic hydroperoxide, demethylation of aminopyrine and oxidation of some substances in perfused rat liver, and their implications for the physiological function of catalase.

Authors:  N Oshino; B Chance
Journal:  Biochem J       Date:  1977-03-15       Impact factor: 3.857

9.  Myocardial H2O2 production in the unanaesthetized rat. Influence of fasting, myocardial load and inhibition of superoxide dismutase and monoamine oxidase.

Authors:  I Kerckaert; F Roels
Journal:  Basic Res Cardiol       Date:  1986 Jan-Feb       Impact factor: 17.165

10.  Inhibitory effects of a novel Val to Thr mutation on the distal heme of human catalase.

Authors:  Zahra Mashhadi; William E Boeglin; Alan R Brash
Journal:  Biochimie       Date:  2014-07-30       Impact factor: 4.079

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