Publication

SnO2-poly(diallyldimethylammonium chloride) films: Electrochemical evidence for heme protein absorption, denaturation, and demetallation

Author(s): Milsom, Elizabeth V. and Dash, Hayley A. and Jenkins, Toby A. and Catherine M. and Thetford, Adam and Bligh, Natalie and Nogala, Wojciech and Opallo, Marcin and Marken, Frank
Title: SnO2-poly(diallyldimethylammonium chloride) films: Electrochemical evidence for heme protein absorption, denaturation, and demetallation
Abstract: Thin mesoporous nanocomposite films of SnO2-poly(diallyidimethylammonium are formed in a layer-by-layer deposition process from SnO2 (nominal 15 nm diameter) and poly(diallyidimethylammonium binder. Atomic force imaging and electron microscopy suggest each deposition cycle is adding ca. 10 nm of chloride) to the film thickness. Data cyclic voltammetry suggest that SnO2-poly(diallyldimethylammonium films are stable and n-type semiconducting but actually sufficiently conducting (similar to mesoporous SnO2) over a range of applied potentials.The immobilization of redox proteins the mesoporous structure is attempted for the heme proteins (bovine) and cytochrome P450(cam) (CYP101). Very similar responses for these systems indicate denaturation in the of polyelectrolyte or the charged SnO2 surface. In addition, it shown that methemoglobin and cytochrome P450(cam) are even to give Fe(III/II) immobilized in electrochemically active within the SnO2-poly(diallyldimethylammonium chloride) film. Most this Fe(III/II) can be sequestered and identified in a test reaction ethylenediaminetetraacetate (EDTA). (C) 2007 Elsevier B.V. All rights reserved.
Pages: 28-36
Journal: JOURNAL OF ELECTROANALYTICAL CHEMISTRY
Publisher: ELSEVIER SCIENCE SA
Addres: PO BOX 564, 1001 LAUSANNE, SWITZERLAND
Volume: 610
ID: ISI:000252014300004
Year: 2007
DOI: 10.1016/j.jelechem.2007.06.021