Phenothiazines are slowly oxidizable substrates of horseradish peroxidase | Zendy

Т. В. Рогожина | Zendy; В. В. Рогожин | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Phenothiazines are slowly oxidizable substrates of horseradish peroxidase

Author(s) -

Т. В. Рогожина,

В. В. Рогожин

Publication year - 2011

Publication title -

biomeditsinskaya khimiya

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.192

H-Index - 15

eISSN - 2310-6972

pISSN - 2310-6905

DOI - 10.18097/pbmc20115705544

Subject(s) - horseradish peroxidase , chemistry , peroxidase , substrate (aquarium) , enzyme kinetics , kinetics , redox , enzyme , nuclear chemistry , inorganic chemistry , organic chemistry , active site , oceanography , physics , quantum mechanics , geology

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research