High-Temperature Electrochemistry of a Solvent-Free Myoglobin Melt

Kamendra P. Sharma, Thomas Risbridger, Kieren Bradley, Adam W. Perriman*, David J. Fermin, Stephen Mann

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

6 Citations (Scopus)

Abstract

The electrochemical responses from a hybrid biofluid comprising lithium hexafluorophosphate (LiPF<inf>6</inf>) dispersed in a solvent-free myoglobin melt are investigated over an extreme temperature range (30-150°C). Incorporation of LiPF<inf>6</inf> 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.

Original languageEnglish
Pages (from-to)976-981
Number of pages6
JournalChemElectroChem
Volume2
Issue number7
DOIs
Publication statusPublished - 15 Jul 2015

Keywords

  • Bioconjugate
  • Lithium hexafluorophosphate
  • Myoglobin
  • Solvent-free
  • Voltammetry

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