کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9890896 | 1540340 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Binding of porphyrin to horseradish peroxidase: Effects on structure and function
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Spectrofluorimetric and spectrophotometric studies were done to understand the binding of hematoporphyrin, a photosensitizer to horseradish peroxidase (EC1.11.1.7). The binding affinity constant (K) decreases as the state of aggregation of the porphyrin increases, while the number of binding sites (approximately 1) remains unchanged. The interaction appears to be mostly hydrophobic, entropy-driven and endothermic process. Hematoporphyrin potentiates horseradish peroxidase-catalyzed H2O2-mediated NADH oxidation, probably by porphyrin-influenced removal of superoxide radicals, which are generated in the system. Conformational change of the protein due to its interaction with porphyrin may be associated with potentiation of the catalytic activity of the enzyme.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 36, Issues 1â2, July 2005, Pages 16-22
Journal: International Journal of Biological Macromolecules - Volume 36, Issues 1â2, July 2005, Pages 16-22
نویسندگان
Susmita Sil, Abhay Sankar Chakraborti,