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Titolo:
Direct electron transfer observed for peroxidase to screen-printed graphite electrodes
Autore:
Schumacher, JT; Hecht, HJ; Dengler, U; Reichelt, J; Bilitewski, U;
Indirizzi:
Natl Res Ctr Biotechnol, Div Biochem Engn, D-38124 Braunschweig, Germany Natl Res Ctr Biotechnol Braunschweig Germany D-38124 aunschweig, Germany Natl Res Ctr Biotechnol, Dept Mol Struct Res, D-38124 Braunschweig, Germany Natl Res Ctr Biotechnol Braunschweig Germany D-38124 aunschweig, Germany
Titolo Testata:
ELECTROANALYSIS
fascicolo: 8-9, volume: 13, anno: 2001,
pagine: 779 - 785
SICI:
1040-0397(200105)13:8-9<779:DETOFP>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
HORSERADISH-PEROXIDASE; HYDROGEN-PEROXIDE; ENZYME ELECTRODES; BIOSENSORS; GLUCOSE; STABILIZATION; REDUCTION; SENSORS; PROGRAM; CARBON;
Keywords:
direct electron transfer; screen-printing; peroxidase; docking simulation; graphite;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Bilitewski, U Natl Res Ctr Biotechnol, Div Biochem Engn, Mascheroder Weg 1, D-38124 Braunschweig, Germany Natl Res Ctr Biotechnol Mascheroder Weg 1 Braunschweig Germany D-38124
Citazione:
J.T. Schumacher et al., "Direct electron transfer observed for peroxidase to screen-printed graphite electrodes", ELECTROANAL, 13(8-9), 2001, pp. 779-785

Abstract

Native and recombinant horseradish peroxidase were immobilized onto screen-printed graphite electrodes by depositing and drying an enzyme solution onto the transduce(-) surface followed by coverage with an UV-polymerizable paste. Direct electron transfer from the transducer to the enzymes was obtained by applying a potential of -100 mV (vs. Ag/AgCl reference electrode) inthe presence of hydrogen peroxide as substrate. Docking of the enzymes to graphite was modelled to estimate the distances from the active site to theelectrode surface. The electrode current was ir creased threefold by adding Gafquat 755N to the enzyme solution. Modelling calculations indicated unspecific but strong binding of Garquat subunits to the protein.

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Documento generato il 27/11/20 alle ore 01:22:56