Literature DB >> 13058869

The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. I. Titration with reducing agents.

P GEORGE.   

Abstract

Entities:  

Keywords:  HYDROGEN PEROXIDE; OXIDASES

Mesh：

Substances：

Year:  1953        PMID： 13058869      PMCID： PMC1268935          DOI： 10.1042/bj0540267

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


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  8 in total

1.  The reaction between metmyoglobin and hydrogen peroxide.

Authors:  P GEORGE; D H IRVINE
Journal:  Biochem J       Date:  1952-11       Impact factor: 3.857

2.  Reaction of methmyoglobin with hydrogen peroxide.

Authors:  P GEORGE; D H IRVINE
Journal:  Nature       Date:  1951-07-28       Impact factor: 49.962

3.  Activity of the cytochrome system in heart muscle preparations.

Authors:  D Keilin; E F Hartree
Journal:  Biochem J       Date:  1947       Impact factor: 3.857

4.  Chemical nature of the secondary hydrogen peroxide compound formed by cytochrome-c peroxidase and horseradish peroxidase.

Authors:  P GEORGE
Journal:  Nature       Date:  1952-04-12       Impact factor: 49.962

5.  Electronic structure of the peroxidase-peroxide complexes.

Authors:  H THEORELL; A EHRENBERG; B CHANCE
Journal:  Arch Biochem Biophys       Date:  1952-05       Impact factor: 4.013

6.  The transition from the primary to the secondary peroxidase-peroxide complex.

Authors:  B CHANCE
Journal:  Arch Biochem Biophys       Date:  1952-05       Impact factor: 4.013

7.  The properties of the enzyme-substrate compounds of horseradish peroxidase and peroxides; the reaction of complex II with ascorbic acid.

Authors:  B CHANCE
Journal:  Arch Biochem       Date:  1949-12

8.  The Properties of the Enzyme-Substrate Compounds of Horse-Radish and Lacto-Peroxidase.

Authors:  B Chance
Journal:  Science       Date:  1949-02-25       Impact factor: 47.728
  8 in total
  24 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.  The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. 2. Formation and decomposition.

Authors:  P GEORGE
Journal:  Biochem J       Date:  1953-09       Impact factor: 3.857

3.  The absorption spectra, magnetic moments and the binding of iron in some haemoproteins.

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

4.  The action of anions on catalase peroxide compounds.

Authors:  P NICHOLLS
Journal:  Biochem J       Date:  1961-11       Impact factor: 3.857

5.  Delayed luminescence of luminol initiated by a membrane-bound peroxidase.

Authors:  Y Ikariyama; S Suzuki; M Aizawa
Journal:  Appl Biochem Biotechnol       Date:  1981-09       Impact factor: 2.926

6.  Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles.

Authors:  I G Gazaryan; N L Klyachko; Y K Dulkis; I V Ouporov; A V Levashov
Journal:  Biochem J       Date:  1997-12-01       Impact factor: 3.857

Review 7.  Oxidation states of peroxidase.

Authors:  I Yamazaki; K Yokota
Journal:  Mol Cell Biochem       Date:  1973-11-15       Impact factor: 3.396

8.  The reaction of azide with catalase and their significance.

Authors:  P Nicholls
Journal:  Biochem J       Date:  1964-02       Impact factor: 3.857

9.  Lipid peroxidation and haemoglobin degradation in red blood cells exposed to t-butyl hydroperoxide. Effects of the hexose monophosphate shunt as mediated by glutathione and ascorbate.

Authors:  R J Trotta; S G Sullivan; A Stern
Journal:  Biochem J       Date:  1982-05-15       Impact factor: 3.857

10.  Lipid peroxidation and haemoglobin degradation in red blood cells exposed to t-butyl hydroperoxide. The relative roles of haem- and glutathione-dependent decomposition of t-butyl hydroperoxide and membrane lipid hydroperoxides in lipid peroxidation and haemolysis.

Authors:  R J Trotta; S G Sullivan; A Stern
Journal:  Biochem J       Date:  1983-06-15       Impact factor: 3.857
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