Literature DB >> 19856293

Protoporphyrin IX potentiates horseradish peroxidase-catalyzed oxidation of NADH:Involvement of enzyme-porphyrin interaction.

S Sil1, A S Chakraborti.   

Abstract

Protoporphyrin IX potentiates horseradish peroxidase-catalyzed hydrogen peroxide-mediated NADH oxidation, but the porphyrin cannot change the enzyme-catalyzed o-dianisidine oxidation. Spectrofluorimetric studies reveal that an interaction occurs between horseradish peroxidase and protoporphyrin IX. The interaction is predominantly hydrophobic and entropy-driven endothermic process. This interaction may influence the potentiation effect of the protoporphyrin IX on horseradish peroxidase-catalyzed NADH oxidation because the latter has a positive correlation with the extent of binding of the protein with the porphyrin.

Entities:  

Year:  1997        PMID: 19856293     DOI: 10.1080/15216549700203191

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN: 1039-9712


  3 in total

Review 1.  Interaction of porphyrins with heme proteins--a brief review.

Authors:  Abhay Sankar Chakraborti
Journal:  Mol Cell Biochem       Date:  2003-11       Impact factor: 3.396

2.  Hematoporphyrin interacts with myoglobin and alters its functions.

Authors:  Susmita Sil; Abhay Sankar Chakraborti
Journal:  Mol Cell Biochem       Date:  2002-08       Impact factor: 3.396

3.  Protoporphyrin IX-induced structural and functional changes in human red blood cells, haemoglobin and myoglobin.

Authors:  Susmita Sil; Tania Bose; Dibyendu Roy; Abhay Sankar Chakraborti
Journal:  J Biosci       Date:  2004-09       Impact factor: 1.826

  3 in total

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