Direct Electron Transfer and Bioelectrocatalysis by a Hexameric, Heme Protein at Nanostructured Electrodes
Journal article
Publication Details
Author list: Tanne J., Jeoung J.H., Peng L., Yarman A., Dietzel B., Schulz B., Schad D., Dobbek H., Wollenberger U., Bier F.F., Scheller F.W.
Journal: Electroanalysis
Publication year: 2015
Volume number: 27
Issue number: 10
Pages: 2262-2267
Publisher: Wiley-VCH Verlag
URL: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84943609754&origin=inward
Languages: English-Great Britain
Abstract
A nanohybrid consisting of poly(3-aminobenzenesulfonic acid-co-aniline) and multiwalled carbon nanotubes [MWCNT-P(ABS-A)]) on a gold electrode was used to immobilize the hexameric tyrosine-coordinated heme protein (HTHP). The enzyme showed direct electron transfer between the heme group of the protein and the nanostructured surface. Desorption of the noncovalently bound heme from the protein could be excluded by control measurements with adsorbed hemin on aminohexanthiol-modified electrodes. The nanostructuring and the optimised charge characteristics resulted in a higher protein coverage as compared with MUA/MU modified electrodes. The adsorbed enzyme shows catalytic activity for the cathodic H2O2 reduction and oxidation of NADH.
