Literature DB >> 238593

A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength.

S Loo, J E Erman.   

Abstract

The rate of the reaction between cytochrome c peroxidase and hydrogen peroxide was investigated using the stopped-flow technique. The apparent bimolecular rate constant was determined between pH 3.3 and pH 11 as a function of ionic strength. The pH dependence of the apparent bimolecular rate constant can be explained by assuming that two ionizable groups on the enzyme strongly influence the rate of the reaction. At 0.1 M ionic strength, a group with a pKa of 5.5 must be unprotonated and a group with a pKa of 9.8 must be protonated for the enzyme to react rapidly with hydrogen peroxide. The apparent acid dissociation constants depend upon the ionic strength. The true bimolecular rate constant has a value of (4.5 +/- 0.3) X 10(7) M-1 sec-1 and is independent of ionic strength.

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Year:  1975        PMID： 238593     DOI： 10.1021/bi00686a027

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


  9 in total

1.  Effect of alternative distal residues on the reactivity of cytochrome c peroxidase: properties of CcP mutants H52D, H52E, H52N, and H52Q.

Authors:  Miriam C Foshay; Lidia B Vitello; James E Erman
Journal:  Biochim Biophys Acta       Date:  2011-02-24

2.  Heme-linked ionizations of myeloperoxidase detected by Raman difference spectroscopy. A comparison with plant and yeast peroxidases.

Authors:  R F Stump; G G Deanin; J M Oliver; J A Shelnutt
Journal:  Biophys J       Date:  1987-04       Impact factor: 4.033

3.  Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants.

Authors:  Anil K Bidwai; Cassandra Meyen; Heather Kilheeney; Damian Wroblewski; Lidia B Vitello; James E Erman
Journal:  Biochim Biophys Acta       Date:  2012-09-25

4.  Kinetic and crystallographic studies of a redesigned manganese-binding site in cytochrome c peroxidase.

Authors:  Thomas D Pfister; Amir Y Mirarefi; Alan J Gengenbach; Xuan Zhao; Connor Danstrom; Nicole Conatser; Yi-Gui Gao; Howard Robinson; Charles F Zukoski; Andrew H-J Wang; Yi Lu
Journal:  J Biol Inorg Chem       Date:  2006-10-05       Impact factor: 3.358

5.  Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase.

Authors:  Jeffrey A Mayfield; Béatrice Blanc; Kenton R Rodgers; Gudrun S Lukat-Rodgers; Jennifer L DuBois
Journal:  Biochemistry       Date:  2013-09-23       Impact factor: 3.162

6.  pH effects on the haem iron co-ordination state in the nitric oxide and deoxy derivatives of ferrous horseradish peroxidase and cytochrome c peroxidase.

Authors:  P Ascenzi; M Brunori; M Coletta; A Desideri
Journal:  Biochem J       Date:  1989-03-01       Impact factor: 3.857

7.  Ferryl derivatives of human indoleamine 2,3-dioxygenase.

Authors:  Changyuan Lu; Syun-Ru Yeh
Journal:  J Biol Chem       Date:  2011-04-18       Impact factor: 5.157

8.  Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pH.

Authors:  Cory M DiCarlo; Lidia B Vitello; James E Erman
Journal:  J Inorg Biochem       Date:  2011-01-09       Impact factor: 4.155

9.  Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site.

Authors:  Naw May Pearl; Timothy Jacobson; Moraa Arisa; Lidia B Vitello; James E Erman
Journal:  Biochemistry       Date:  2007-06-20       Impact factor: 3.162
  9 in total

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