کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
30464 44480 2013 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Binding of chrysoidine to catalase: Spectroscopy, isothermal titration calorimetry and molecular docking studies
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Binding of chrysoidine to catalase: Spectroscopy, isothermal titration calorimetry and molecular docking studies
چکیده انگلیسی


• Chrysoidine inhibits catalase in a non-competitive manner.
• No profound conformational change of catalase occurs in the presence of chrysoidine.
• ITC results indicate that catalase has two sets of binding sites for chrysoidine.
• Chrysoidine is located within the bottleneck in the main channel of catalase.
• We report a strategy to investigate the toxicity of chrysoidine at the molecular level.

Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become an environmental concern due to its negative effects on human beings. In this work, the interactions between chrysoidine and bovine liver catalase (BLC) were explored. Obvious loss in catalytic activity was observed after incubation of BLC with chrysoidine, and the inhibition effect of BLC was found to be of the non-competitive type. No profound conformational change of BLC occurs in the presence of chrysoidine as revealed by UV–vis absorption, circular dichroism and fluorescence spectroscopy studies. Isothermal titration calorimetry results indicate that catalase has two sets of binding sites for chrysoidine. Further, molecular docking simulations show that chrysoidine is located within the bottleneck in the main channel of the substrate to the active site of BLC, which explain the activity inhibition of BLC by chrysoidine.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 128, 5 November 2013, Pages 35–42
نویسندگان
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