Abstract
Redox-active cytochromeb562with a tethered azide group on the heme propionate side chain is covalently linked to an acetylene moiety introduced on the sidewall of a single-walled carbon nanotube by copper-catalyzed click chemistry.
Highlights
Redox-active cytochrome b562 with a tethered azide group on the heme propionate side chain is covalently linked to an acetylene moiety introduced on the sidewall of a single-walled carbon nanotube (SWNT) by copper-catalyzed click chemistry forming a triazole ring with the heme active site directly linked to the SWNT
The sample prepared without CuSO4 does not have similar redox peaks. These results clearly indicate that the strategy for combining SWNT and cytochrome b562 (CYT) in the CuAAC reaction provides stable hybrids which are linked by a triazole moiety
Cytochrome b562 with a tethered azide group on the heme propionate side chain was covalently linked to the acetylene moiety introduced on the sidewall of SWNT via a speci c covalent bond containing the triazole ring formed by copper-catalyzed click chemistry
Summary
Redox-active cytochrome b562 with a tethered azide group on the heme propionate side chain is covalently linked to an acetylene moiety introduced on the sidewall of a single-walled carbon nanotube (SWNT) by copper-catalyzed click chemistry forming a triazole ring with the heme active site directly linked to the SWNT. Redox-active hemoproteins form a major class of enzymes that are useful for constructing enzyme-immobilized electrodes due to their diverse functions including electron transfer, catalysis, and sensing.[15,16,17,18,19,20,21,22,23,24,25] Many hemoproteins possess a replaceable heme b cofactor in the heme pocket, enabling immobilization on the electrode via the heme–heme pocket interaction.[26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45] In this paper, we demonstrate speci cally oriented covalent immobilization of azide-linked cytochrome b562 (CYT) on the sidewall of SWNT using the CuAAC reaction (Fig. 1).
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