Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode

Hanyu Wang; Alexander Johs; James F. Browning; David Alan Tennant; Liyuan Liang

doi:10.1016/j.bioelechem.2019.05.012

Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode

Hanyu Wang, Alexander Johs, James F. Browning, David Alan Tennant, Liyuan Liang

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k°_ET, of 0.4 s⁻¹ for the native form and 0.55 s⁻¹ for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k°_ET = 8.0·10⁻³ cm·s⁻¹ at pH 7.07. Modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications for describing chemical transformations at biological-mineral interfaces.

Original language	English
Pages (from-to)	162-169
Number of pages	8
Journal	Bioelectrochemistry
Volume	129
DOIs	https://doi.org/10.1016/j.bioelechem.2019.05.012
State	Published - Oct 2019

Funding

This research was sponsored by the Laboratory Directed Research and Development Program of Oak Ridge National Laboratory, managed by UT-Battelle, LLC, for the U.S. Department of Energy (Project ID 8174), under Contract No. DE-AC05-00OR22725 with the U.S. Department of Energy. The United States Government retains and the publisher, by accepting the article for publication, acknowledges that the United States Government retains a non-exclusive, paid-up, irrevocable, worldwide license to publish or reproduce the published form of this manuscript, or allow others to do so, for United States Government purposes. The Department of Energy will provide public access to these results of federally sponsored research in accordance with the DOE Public Access Plan (http://energy.gov/downloads/doe-public-access-plan). This research was sponsored by the Laboratory Directed Research and Development Program of Oak Ridge National Laboratory , managed by UT-Battelle, LLC, for the U.S. Department of Energy (Project ID 8174), under Contract No. DE-AC05-00OR22725 with the U.S. Department of Energy. The United States Government retains and the publisher, by accepting the article for publication, acknowledges that the United States Government retains a non-exclusive, paid-up, irrevocable, worldwide license to publish or reproduce the published form of this manuscript, or allow others to do so, for United States Government purposes. The Department of Energy will provide public access to these results of federally sponsored research in accordance with the DOE Public Access Plan ( http://energy.gov/downloads/doe-public-access-plan ).

Keywords

Adsorption
Cyclic voltammetry
Cytochrome
Electron transfer
Hematite

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10.1016/j.bioelechem.2019.05.012

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title = "Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode",

abstract = "We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k°ET, of 0.4 s−1 for the native form and 0.55 s−1 for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k°ET = 8.0·10−3 cm·s−1 at pH 7.07. Modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications for describing chemical transformations at biological-mineral interfaces.",

keywords = "Adsorption, Cyclic voltammetry, Cytochrome, Electron transfer, Hematite",

author = "Hanyu Wang and Alexander Johs and Browning, {James F.} and Tennant, {David Alan} and Liyuan Liang",

note = "Publisher Copyright: {\textcopyright} 2019",

year = "2019",

month = oct,

doi = "10.1016/j.bioelechem.2019.05.012",

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AU - Wang, Hanyu

AU - Johs, Alexander

AU - Browning, James F.

AU - Tennant, David Alan

AU - Liang, Liyuan

PY - 2019/10

Y1 - 2019/10

N2 - We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k°ET, of 0.4 s−1 for the native form and 0.55 s−1 for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k°ET = 8.0·10−3 cm·s−1 at pH 7.07. Modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications for describing chemical transformations at biological-mineral interfaces.

AB - We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k°ET, of 0.4 s−1 for the native form and 0.55 s−1 for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k°ET = 8.0·10−3 cm·s−1 at pH 7.07. Modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications for describing chemical transformations at biological-mineral interfaces.

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Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode

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