Phenothiazines are slowly oxidizable substrates of horseradish peroxidase

Rogozhina T.V.1, Rogozhin V.V.1

1. Yakutsk State Agricultural Academy
Section: Experimental/Clinical Study
DOI: 10.18097/PBMC20115705544      PubMed Id: 22629605
Year: 2011  Volume: 57  Issue: 5  Pages: 544-553
Reactions of peroxidase oxidation of triftazine and thioproperazine have been investigated in the presence of horseradish peroxidase using steady state kinetic methods. It has been shown that phenothiazines are slowly oxidizable substrates for horseradish peroxidase. kcat and Km values have been determined in the range of pH from 4.5 to 7.5. The study of co-oxidation of phenothiazines and o-dianisidine (ODN) revealed that in the presence of aminazine and ODN in the reaction medium both substances follow sequential oxidation. ODN oxidation was not observed until full conversion of aminazine. At pH 4.5-5.5 thioproperazine bound to the enzyme-substrate complex and caused a nticompetitive inhibition of peroxidase. At pH>5.5 sequential substrate oxidation with preferential thioproperazine conversion occurred. In the range of pH from 4.5 to 7.5 triftazine did not influence ODN oxidation.
Download PDF:
Keywords: horseradish peroxidase, triftazine, thioproperazine, aminazine, o-dianisidine, phenothiazines

Rogozhina, T. V., Rogozhin, V. V. (2011). Phenothiazines are slowly oxidizable substrates of horseradish peroxidase. Biomeditsinskaya khimiya, 57(5), 544-553.
This paper is also available as the English translation: 10.1134/S1990750811040093
 2019 (vol 65)
 2018 (vol 64)
 2017 (vol 63)
 2016 (vol 62)
 2015 (vol 61)
 2014 (vol 60)
 2013 (vol 59)
 2012 (vol 58)
 2011 (vol 57)
 2010 (vol 56)
 2009 (vol 55)
 2008 (vol 54)
 2007 (vol 53)
 2006 (vol 52)
 2005 (vol 51)
 2004 (vol 50)
 2003 (vol 49)