کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9758941 | 1496933 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Direct electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
الکتروشیمی
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چکیده انگلیسی
Direct electrochemistry of heme multicofactor-containing enzymes, e.g., microbial theophylline oxidase (ThOx) and d-fructose dehydrogenase (FDH) from Gluconobacter industrius was studied on alkanethiol-modified gold electrodes and was compared with that of some previously studied complex heme enzymes, specifically, cellobiose dehydrogenase (CDH) and sulphite oxidase (SOx). The formal redox potentials for enzymes in direct electronic communication varied for ThOx from â112 to â101 mV (vs. Ag|AgCl), at pH 7.0, and for FDH from â158 to â89 mV, at pH 5.0 and pH 4.0, respectively, on differently charged alkanethiol layers. Direct and mediated by cytochrome c electrochemistry of FDH correlated with the existence of two active centres in the protein structure, i.e., the heme and the pyrroloquinoline quinone (PQQ) prosthetic groups. The effect of the alkanethiols of different polarity and charge on the surface properties of the gold electrodes necessary for adsorption and orientation of ThOx, FDH, CDH and SOx, favourable for the efficient electrode-enzyme electron transfer reaction, is discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioelectrochemistry - Volume 66, Issues 1â2, April 2005, Pages 55-63
Journal: Bioelectrochemistry - Volume 66, Issues 1â2, April 2005, Pages 55-63
نویسندگان
Elena E. Ferapontova, Lo Gorton,