Literature DB >> 4477954

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

P Jones, D N Middlemiss.   

Abstract

Studies of the pH decreases that accompany the formation of Compound I from ox liver catalase and peroxoacetic acid in unbuffered systems imply that 1 mol of acetic acid is released/mol of catalase ferrihaem Compound I formed. This result is consistent with results previously obtained (Schonbaum & Lo, 1972) for the formation of peroxidase Compound I by using peroxo acid substrate.

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Year:  1974        PMID： 4477954      PMCID： PMC1168406          DOI： 10.1042/bj1430473

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


  3 in total

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

Authors:  P Jones; D N Middlemiss
Journal:  Biochem J       Date:  1972-11       Impact factor: 3.857

2.  Peroxidatic activity of catalase.

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

3.  Interaction of peroxidases with aromatic peracids and alkyl peroxides. Product analysis.

Authors:  G R Schonbaum; S Lo
Journal:  J Biol Chem       Date:  1972-05-25       Impact factor: 5.157
  3 in total
  2 in total

1.  Stereospecific haem cleavage. A model for the formation of bile-pigment isomers in vivo and in vitro.

Authors:  S B Brown
Journal:  Biochem J       Date:  1976-10-01       Impact factor: 3.857

2.  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 in total

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