DDirect electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes

被引:48
作者
Ferapontova, EE
Gorton, L
机构
[1] Lund Univ, Dept Analyt Chem, SE-22100 Lund, Sweden
[2] Weblab, IT Ctr, Grp Bioinformat, Novosibirsk 630102, Russia
[3] Lund Univ, Dept Analyt Chem, SE-22100 Lund, Sweden
关键词
theophylline oxidase; D-fructose dehydrogenase; heme; direct electron transfer; alkanethiol self-assembled monolayers;
D O I
10.1016/j.bioelechem.2004.04.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 -112 to -101 mV (vs. Ag vertical bar AgCl), at pH 7.0, and for FDH from - 158 to -89 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 g-old electrodes necessary for adsorption and orientation of ThOx, FDH, CDH and SOx, favourable for the efficient electrode-enzyme electron transfer reaction, is discussed. (c) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:55 / 63
页数:9
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