<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Parthasarathy, Meera</style></author><author><style face="normal" font="default" size="100%">Pillai, Vijayamohanan K.</style></author><author><style face="normal" font="default" size="100%">Mulla, Imtiaz S.</style></author><author><style face="normal" font="default" size="100%">Shabab, Mohammed</style></author><author><style face="normal" font="default" size="100%">Khan, Mohammad Islam</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">All-solid-state' electrochemistry of a protein-confined polymer electrolyte film</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemical and Biophysical Research Communications</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">all-solid-state</style></keyword><keyword><style  face="normal" font="default" size="100%">cyclic voltammetry</style></keyword><keyword><style  face="normal" font="default" size="100%">hemoglobin</style></keyword><keyword><style  face="normal" font="default" size="100%">Impedance</style></keyword><keyword><style  face="normal" font="default" size="100%">Nafion</style></keyword><keyword><style  face="normal" font="default" size="100%">redox behavior</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">ACADEMIC PRESS INC ELSEVIER SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA</style></pub-location><volume><style face="normal" font="default" size="100%">364</style></volume><pages><style face="normal" font="default" size="100%">86-91</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Interfacial redox behavior of a heme protein (hemoglobin) confined in a solid polymer electrolyte membrane, Nafion (a perfluoro sulfonic acid ionomer) is investigated using a unique `all-solid-state' electrochemical methodology. The supple phase-separated structure of the polymer electrolyte membrane, with hydrophilic pools containing solvated protons and water molecules, is found to preserve the incorporated protein in its active form even in the solid-state, using UV-visible, Fluorescence (of Tryptophan and Tyrosine residues) and DRIFT (diffuse reflectance infrared Fourier transform) spectroscopy. More specifically, solid-state cyclic voltammetry and electrochemical impedance of the protein-incorporated polymer films reveal that the Fe2+-form of the entrapped protein is found to bind molecular oxygen more strongly than the native protein. In the `all-solid-state' methodology, as there is no need to dip the protein-modified electrode in a liquid electrolyte (like the conventional electrochemical methods), it offers an easier means to study a number of proteins in a variety of polymer matrices (even biomimetic assemblies). In addition, the results of the present investigation could find interesting application in a variety of research disciplines, in addition to its fundamental scientific interest, including protein biotechnology, pharmaceutical and biomimetic chemistry. (C) 2007 Elsevier Inc. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.371</style></custom4></record></records></xml>