Payame Noor University Experimental animal Biology 2322-2387 6 4 2018 05 22 Kinetics studies of peroxidase enzyme in the presence of ferric oxide and copper oxide at difference temperatures Kinetics studies of peroxidase enzyme in the presence of ferric oxide and copper oxide at difference temperatures 23 33 4725 FA Behzad Shareghi Academic staff/ Shahrekord university Maryam Kazemi Nafchi M. Sc. Student of Biochemistry, Shahrekord University, Iran Journal Article 2018 06 17 <strong>Abstract</strong> <br />Peroxidases are a group of oxidoreductases that are produced by a number of microorganisms and plants, and catalyse the reduction of peroxides. Peroxidases are widely used in clinical biochemistry and enzyme immunoassay. Horseradish peroxidase isoenzyme C (HRPC) is one of the characterized peroxidases. The structure of the enzyme is largely alpha helical. Peroxidase enzyme is detox important enzyme that to work process for getting rid of the cells of additional hydrogen peroxide under normal and stress conditions, including contamination with toxic levels of heavy metals, however, severe stress possible influence upon the activity of detoxification enzyme. Kinetics studies of peroxidase enzyme were performed using a spectrophotometer UV-Vis fitted with electronic control system at 35 °C and 45 °C and pH4 and in the presence ferric oxide and copper oxide. Kinetic parameters show that ferric oxide and copper oxide becomes caused the decrease of maximum speed (V_MAX) and activity of the enzyme. Likely due to the ferri and copper ions have positively charged, these places are on or near the sites of glycosylation of enzyme and by their negatively charged are suitable binding sites for iron and copper. Likely binding of iron and copper are caused more changes of the secondary structure and makes random coil deduction more than alpha helix. <strong>Abstract</strong> <br />Peroxidases are a group of oxidoreductases that are produced by a number of microorganisms and plants, and catalyse the reduction of peroxides. Peroxidases are widely used in clinical biochemistry and enzyme immunoassay. Horseradish peroxidase isoenzyme C (HRPC) is one of the characterized peroxidases. The structure of the enzyme is largely alpha helical. Peroxidase enzyme is detox important enzyme that to work process for getting rid of the cells of additional hydrogen peroxide under normal and stress conditions, including contamination with toxic levels of heavy metals, however, severe stress possible influence upon the activity of detoxification enzyme. Kinetics studies of peroxidase enzyme were performed using a spectrophotometer UV-Vis fitted with electronic control system at 35 °C and 45 °C and pH4 and in the presence ferric oxide and copper oxide. Kinetic parameters show that ferric oxide and copper oxide becomes caused the decrease of maximum speed (V_MAX) and activity of the enzyme. Likely due to the ferri and copper ions have positively charged, these places are on or near the sites of glycosylation of enzyme and by their negatively charged are suitable binding sites for iron and copper. Likely binding of iron and copper are caused more changes of the secondary structure and makes random coil deduction more than alpha helix. https://eab.journals.pnu.ac.ir/article_4725_3595c19f5cfd01f5abb1a3e70b5fef25.pdf