High-Temperature Electrochemistry of a Solvent-Free Myoglobin Melt

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

doi:10.1002/celc.201500094

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 journal › Article (Academic Journal) › peer-review

8 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 language	English
Pages (from-to)	976-981
Number of pages	6
Journal	ChemElectroChem
Volume	2
Issue number	7
DOIs	https://doi.org/10.1002/celc.201500094
Publication status	Published - 15 Jul 2015

Research Groups and Themes

Physical & Theoretical
Inorganic & Materials

Keywords

Bioconjugate
Lithium hexafluorophosphate
Myoglobin
Solvent-free
Voltammetry

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@article{968685a1dfcc4f24b28f1a761ffca339,

title = "High-Temperature Electrochemistry of a Solvent-Free Myoglobin Melt",

abstract = "The electrochemical responses from a hybrid biofluid comprising lithium hexafluorophosphate (LiPF6) dispersed in a solvent-free myoglobin melt are investigated over an extreme temperature range (30-150°C). Incorporation of LiPF6 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.",

keywords = "Bioconjugate, Lithium hexafluorophosphate, Myoglobin, Solvent-free, Voltammetry",

author = "Sharma, \{Kamendra P.\} and Thomas Risbridger and Kieren Bradley and Perriman, \{Adam W.\} and Fermin, \{David J.\} and Stephen Mann",

year = "2015",

month = jul,

day = "15",

doi = "10.1002/celc.201500094",

language = "English",

volume = "2",

pages = "976--981",

journal = "ChemElectroChem",

issn = "2196-0216",

publisher = "John Wiley \& Sons, Ltd.",

number = "7",

}

TY - JOUR

T1 - High-Temperature Electrochemistry of a Solvent-Free Myoglobin Melt

AU - Sharma, Kamendra P.

AU - Risbridger, Thomas

AU - Bradley, Kieren

AU - Perriman, Adam W.

AU - Fermin, David J.

AU - Mann, Stephen

PY - 2015/7/15

Y1 - 2015/7/15

N2 - The electrochemical responses from a hybrid biofluid comprising lithium hexafluorophosphate (LiPF6) dispersed in a solvent-free myoglobin melt are investigated over an extreme temperature range (30-150°C). Incorporation of LiPF6 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.

AB - The electrochemical responses from a hybrid biofluid comprising lithium hexafluorophosphate (LiPF6) dispersed in a solvent-free myoglobin melt are investigated over an extreme temperature range (30-150°C). Incorporation of LiPF6 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.

KW - Bioconjugate

KW - Lithium hexafluorophosphate

KW - Myoglobin

KW - Solvent-free

KW - Voltammetry

UR - https://www.scopus.com/pages/publications/84938578195

U2 - 10.1002/celc.201500094

DO - 10.1002/celc.201500094

M3 - Article (Academic Journal)

AN - SCOPUS:84938578195

SN - 2196-0216

VL - 2

SP - 976

EP - 981

JO - ChemElectroChem

JF - ChemElectroChem

IS - 7

ER -

High-Temperature Electrochemistry of a Solvent-Free Myoglobin Melt

Abstract

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Functional Biomolecular Liquids

Molten Proteins: synthesis and design of novel biomolecule-based liquid nanomaterials and their application in bionanochemistry

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High-Temperature Electrochemistry of a Solvent-Free Myoglobin Melt

Abstract

Research Groups and Themes

Keywords

Access to Document

Handle.net

Other files and links

Fingerprint

Projects

Functional Biomolecular Liquids

Molten Proteins: synthesis and design of novel biomolecule-based liquid nanomaterials and their application in bionanochemistry

Cite this