Literature DB >> 4664571

Formation of compound I by the reaction of catalase with peroxoacetic acid.

P Jones, D N Middlemiss.   

Abstract

1. The formation of Compound I by the reactions of bacterial and ox liver catalases with peroxoacetic acid was examined. In both cases the process occurs almost entirely by reaction of catalase with un-ionized peroxoacetic acid molecules. The result suggests an important role for the bound peroxidic proton in the enzyme-substrate interaction. 2. The peroxidatic properties of the Compounds I formed when peroxoacetic acid was used were examined by studying the oxidations of ethanol and formate; the results closely resemble those previously reported when H(2)O(2) and alkyl hydroperoxides were used. 3. Compound I formed with bacterial catalase and peroxoacetic acid is remarkably stable in the absence of added donor and the preparation has considerable potential for detailed studies of the nature of this intermediate.

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Year:  1972        PMID: 4664571      PMCID: PMC1174420          DOI: 10.1042/bj1300411

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


  9 in total

1.  Primary compounds of catalase and peroxidase.

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

2.  The enzymesubstrate compounds of bacterial catalase and peroxides.

Authors:  B CHANCE; D HERBERT
Journal:  Biochem J       Date:  1950-04       Impact factor: 3.857

Review 3.  Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.

Authors:  A Deisseroth; A L Dounce
Journal:  Physiol Rev       Date:  1970-07       Impact factor: 37.312

4.  The catalase-hydrogen peroxide system. Role of sub-units in the thermal deactivation of bacterial catalase in the absence of substrate.

Authors:  P Jones; A Suggett
Journal:  Biochem J       Date:  1968-08       Impact factor: 3.857

5.  The catalase-hydrogen peroxide system. A theoretical appraisal of the mechanism of catalase action.

Authors:  P Jones; A Suggett
Journal:  Biochem J       Date:  1968-12       Impact factor: 3.857

6.  Catalatic activity of iron(3)-centred catalysts. Role of dimerization in the catalytic action of ferrihaems.

Authors:  S B Brown; T C Dean; P Jones
Journal:  Biochem J       Date:  1970-05       Impact factor: 3.857

7.  Peroxidatic activity of catalase.

Authors:  M L Kremer
Journal:  Biochim Biophys Acta       Date:  1970-02-11

8.  Dissociation of catalase. A correlation between changes in sedimentation and spectroscopic properties accompanying dissociation of bacterial catalase in alkaline solution.

Authors:  P Jones; R H Pain; A Suggett
Journal:  Biochem J       Date:  1970-06       Impact factor: 3.857

9.  The peroxidase activity of deuterohemin.

Authors:  D Portsmouth; E A Beal
Journal:  Eur J Biochem       Date:  1971-04-30
  9 in total
  7 in total

1.  The kinetics of formation of horseradish peroxidase compound I by reaction with peroxobenzoic acids. pH and peroxo acid substituent effects.

Authors:  D M Davies; P Jones; D Mantle
Journal:  Biochem J       Date:  1976-07-01       Impact factor: 3.857

2.  Relationship Between Main Channel Structure of Catalases and the Evolutionary Direction in Cold-Adapted Hydrogen Peroxide-Tolerant Exiguobacteium and Psychrobacter.

Authors:  Yoshiko Hanaoka; Hideyuki Kimoto; Kazuaki Yoshimume; Isao Hara; Hidetoshi Matsuyama; Isao Yumoto
Journal:  Indian J Microbiol       Date:  2020-05-06       Impact factor: 2.461

3.  Formation of catalase compound I by reaction with peroxoacetic acid: pH changes in unbuffered systems.

Authors:  P Jones; D N Middlemiss
Journal:  Biochem J       Date:  1974-11       Impact factor: 3.857

4.  Cold adapted features of Vibrio salmonicida catalase: characterisation and comparison to the mesophilic counterpart from Proteus mirabilis.

Authors:  Marit Sjo Lorentzen; Elin Moe; Hélène Marie Jouve; Nils Peder Willassen
Journal:  Extremophiles       Date:  2006-04-12       Impact factor: 2.395

5.  Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2.

Authors:  J Hernández-Ruiz; M B Arnao; A N Hiner; F García-Cánovas; M Acosta
Journal:  Biochem J       Date:  2001-02-15       Impact factor: 3.857

6.  Role of radical formation at tyrosine 193 in the allene oxide synthase domain of a lipoxygenase-AOS fusion protein from coral.

Authors:  Fayi Wu; Leron J Katsir; Margaret Seavy; Betty J Gaffney
Journal:  Biochemistry       Date:  2003-06-10       Impact factor: 3.162

7.  The catalase activity of ferrihaems.

Authors:  P Jones; T Robson; S B Brown
Journal:  Biochem J       Date:  1973-10       Impact factor: 3.857

  7 in total

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