Literature DB >> 4764267

The catalase activity of ferrihaems.

P Jones, T Robson, S B Brown.   

Abstract

1. The variation of the specific stoicheiometric catalatic activity of proto- and deuteroferrihaem with total ferrihaem concentration has been studied at 25 degrees C over a wide range of pH. For deuteroferrihaem the results imply that only monomeric ferrihaem species contribute significantly to the catalatic activity. Protoferrihaem is more highly dimerized in solution and, in this system, contributions to the catalatic activity from both monomeric and dimeric ferrihaem species were observed. The ratio of the specific activity of protoferrihaem monomer to that of dimer varied from approximately 20 at pH7 to 5x10(4) at pH12.2. 2. The specific activity of protoferrihaem monomer closely resembles that of deuteroferrihaem monomer, both in magnitude and pH-dependence. In both cases the activity is inversely proportional to [H(+)]. In contrast, the activity of catalase is independent of pH in the range 5-10. At pH13 the activity of ferrihaem monomer becomes equal to the maximal activity of catalase. The results are in good agreement with those reported by Brown et al. (1970b) and provide support for the assumptions upon which this previous analysis relied. 3. Information from the literature concerning the catalatic activity and dimerization of the iron(III) complex of 4,4',4'',4'''-tetrasulphophthalocyanine (Waldmeier & Sigel, 1971; Sigel et al., 1971) have been re-analysed. The results imply that both the monomeric and dimeric complexes contribute to catalatic activity and these activities closely resemble those of the corresponding protoferrihaem species.

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Year:  1973        PMID: 4764267      PMCID: PMC1165830          DOI: 10.1042/bj1350353

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


  10 in total

1.  Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions.

Authors:  D KEILIN; E F HARTREE
Journal:  Biochem J       Date:  1955-06       Impact factor: 3.857

2.  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

3.  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

4.  The catalse-hydrogen peroxide system. Kinetics of catalatic action at high substrate concentrations.

Authors:  P Jones; A Suggett
Journal:  Biochem J       Date:  1968-12       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.  Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution.

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

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.  Infrared evidence for an oxo-bridged (Fe-O-Fe) haemin dimer.

Authors:  S B Brown; P Jones; I R Lantzke
Journal:  Nature       Date:  1969-08-30       Impact factor: 49.962

10.  Thermodynamic and kinetic properties of an iron-porphyrin system.

Authors:  E B Fleischer; J M Palmer; T S Srivastava; A Chatterjee
Journal:  J Am Chem Soc       Date:  1971-06-30       Impact factor: 15.419

  10 in total
  9 in total

1.  Detection of heme-binding proteins in epidemic strains of Burkholderia cepacia.

Authors:  J W Smalley; P Charalabous; A J Birss; C A Hart
Journal:  Clin Diagn Lab Immunol       Date:  2001-05

2.  Interactions of Porphyromonas gingivalis with oxyhaemoglobin and deoxyhaemoglobin.

Authors:  John W Smalley; Andrew J Birss; Robert Withnall; Jack Silver
Journal:  Biochem J       Date:  2002-02-15       Impact factor: 3.857

3.  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

4.  Haemoglobin catabolism: the role of ferrihaems in studies of the degradation pathway.

Authors:  N A Brown; R F King; M E Shillcock; S B Brown
Journal:  Biochem J       Date:  1974-01       Impact factor: 3.857

5.  Catalase model systems. Decomposition of hydrogen peroxide catalysed by mesoferrihaem, deuteroferrihaem, coproferrihaem and haematoferrihaem.

Authors:  H Hatzikonstantinou; S B Brown
Journal:  Biochem J       Date:  1978-09-15       Impact factor: 3.857

6.  Oxidation of deuteroferrihaem by hydrogen peroxide.

Authors:  P Jones; K Prudhoe; T Robson
Journal:  Biochem J       Date:  1973-10       Impact factor: 3.857

7.  The pH dependence of the mechanism of reaction of hydrogen peroxide with a nonaggregating, non-mu-oxo dimer-forming iron (III) porphyrin in water.

Authors:  T C Bruice; M F Zipplies; W A Lee
Journal:  Proc Natl Acad Sci U S A       Date:  1986-07       Impact factor: 11.205

8.  A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin.

Authors:  John W Smalley; Michael F Thomas; Andrew J Birss; Robert Withnall; Jack Silver
Journal:  Biochem J       Date:  2004-05-01       Impact factor: 3.857

9.  Equilibrium and kinetic studies of the aggregation of porphyrins in aqueous solution.

Authors:  S B Brown; M Shillcock; P Jones
Journal:  Biochem J       Date:  1976-02-01       Impact factor: 3.766

  9 in total

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