A Voltammetric Perspective of Multi-Electron and Proton Transfer in Protein Redox Chemistry: Insights From Computational Analysis of Escherichia coli HypD Fourier Transformed Alternating Current Voltammetry

TY - JOUR

T1 - A Voltammetric Perspective of Multi-Electron and Proton Transfer in Protein Redox Chemistry:

T2 - Insights From Computational Analysis of Escherichia coli HypD Fourier Transformed Alternating Current Voltammetry

AU - Dale-Evans, Alister R.

AU - Robinson, Martin J.

AU - Lloyd-Laney, Henry O.

AU - Gavaghan, David J.

AU - Bond, Alan M.

AU - Parkin, Alison

N1 - © 2021 Dale-Evans, Robinson, Lloyd-Laney, Gavaghan, Bond and Parkin.

PY - 2021/6/14

Y1 - 2021/6/14

N2 - This paper explores the impact of pH on the mechanism of reversible disulfide bond (CysS-SCys) reductive breaking and oxidative formation in Escherichia coli hydrogenase maturation factor HypD, a protein which forms a highly stable adsorbed film on a graphite electrode. To achieve this, low frequency (8.96 Hz) Fourier transformed alternating current voltammetric (FTACV) experimental data was used in combination with modelling approaches based on Butler-Volmer theory with a dual polynomial capacitance model, utilizing an automated two-step fitting process conducted within a Bayesian framework. We previously showed that at pH 6.0 the protein data is best modelled by a redox reaction of two separate, stepwise one-electron, one-proton transfers with slightly “crossed” apparent reduction potentials that incorporate electron and proton transfer terms (E0app2 > E0app1). Remarkably, rather than collapsing to a concerted two-electron redox reaction at more extreme pH, the same two-stepwise one-electron transfer model with E0app2 > E0app1 continues to provide the best fit to FTACV data measured across a proton concentration range from pH 4.0 to pH 9.0. A similar, small level of crossover in reversible potentials is also displayed in overall two-electron transitions in other proteins and enzymes, and this provides access to a small but finite amount of the one electron reduced intermediate state.

AB - This paper explores the impact of pH on the mechanism of reversible disulfide bond (CysS-SCys) reductive breaking and oxidative formation in Escherichia coli hydrogenase maturation factor HypD, a protein which forms a highly stable adsorbed film on a graphite electrode. To achieve this, low frequency (8.96 Hz) Fourier transformed alternating current voltammetric (FTACV) experimental data was used in combination with modelling approaches based on Butler-Volmer theory with a dual polynomial capacitance model, utilizing an automated two-step fitting process conducted within a Bayesian framework. We previously showed that at pH 6.0 the protein data is best modelled by a redox reaction of two separate, stepwise one-electron, one-proton transfers with slightly “crossed” apparent reduction potentials that incorporate electron and proton transfer terms (E0app2 > E0app1). Remarkably, rather than collapsing to a concerted two-electron redox reaction at more extreme pH, the same two-stepwise one-electron transfer model with E0app2 > E0app1 continues to provide the best fit to FTACV data measured across a proton concentration range from pH 4.0 to pH 9.0. A similar, small level of crossover in reversible potentials is also displayed in overall two-electron transitions in other proteins and enzymes, and this provides access to a small but finite amount of the one electron reduced intermediate state.

U2 - 10.3389/fchem.2021.672831

DO - 10.3389/fchem.2021.672831

M3 - Article

VL - 9

JO - Frontiers in Chemistry

JF - Frontiers in Chemistry

SN - 2296-2646

M1 - 672831

ER -