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High‐Temperature Electrochemistry of a Solvent‐Free Myoglobin Melt
Author(s) -
Sharma Kamendra P.,
Risbridger Thomas,
Bradley Kieren,
Perriman Adam W.,
Fermin David J.,
Mann Stephen
Publication year - 2015
Publication title -
chemelectrochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.182
H-Index - 59
ISSN - 2196-0216
DOI - 10.1002/celc.201500094
Subject(s) - myoglobin , chemistry , electrochemistry , hexafluorophosphate , solvent , heme , atmospheric temperature range , redox , inorganic chemistry , organic chemistry , electrode , thermodynamics , catalysis , ionic liquid , physics , enzyme
The electrochemical responses from a hybrid biofluid comprising lithium hexafluorophosphate (LiPF 6 ) dispersed in a solvent‐free myoglobin melt are investigated over an extreme temperature range (30–150 °C). Incorporation of LiPF 6 resulted in an approximately 20‐fold increase in the conductivity of the biofluid across the entire temperature range. A polaron‐type mechanism involving electron hopping from heme‐to‐heme centers of myoglobin, accompanied by extrinsic Li counter‐ion movement, is proposed for the charge‐transport kinetics in the solvent‐free melt. Significantly, the redox signature of the heme prosthetic group varied systematically and reversibly with temperature, which was consistent with hyperthermophilic unfolding/refolding of the protein structure.