Thermodynamics and kinetics of reduction and species conversion at a hydrophobic surface for mitochondrial cytochromes c and their cardiolipin adducts

Ranieri, Antonio; Rocco, Giulia Di; Millo, Diego; Battistuzzi, Gianantonio; Bortolotti, Carlo Augusto; Lancellotti, Lidia; Borsari, Marco; Sola, Marcó

doi:10.1016/j.electacta.2015.07.065

Cited by 16 publications

(48 citation statements)

References 64 publications

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“…[1][2][3][4][5]33,34,38,39] A number of studies obtained the right orientation of ET proteins and redox enzymes using electrode (mainly Au) surfaces functionalized with self-assembled thiol monolayers or with spacers of variable lengths bearing endgroups of different nature. [1][2][3][29][30][31] Some proteins, moreover, such as nitrate reductase, [29,48] DMSO reductase [29] cytochrome c nitrite reductase, [49,50] sulfite oxidase, [51,52] cytochrome c [53,54] and cytochrome c 3 , [55] upon electron transfer process undergo more or less severe conformational changes (which, in turn, can modulate the following catalytic process). In a short time scale, typical of a CV measurement, the protein transfers electrons with the electrode without diffusing through the film.…”

Section: Bioelectrocatalysismentioning

confidence: 99%

“…[54,73,131,157,[163][164][165][166][167]190,194] HTHP (hexameric tyrosine-coordinated heme protein) electrostatically immobilized on negatively charged SAMs is an efficient electrocatalyst towards peroxide reduction and enzymatic oxidation of NADH. [54,73,131,157,[163][164][165][166][167]190,194] HTHP (hexameric tyrosine-coordinated heme protein) electrostatically immobilized on negatively charged SAMs is an efficient electrocatalyst towards peroxide reduction and enzymatic oxidation of NADH.…”

Section: Other Proteinsmentioning

confidence: 99%

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Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

et al. 2019

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Heme proteins encompass redox enzymes, electron transferases, and species for dioxygen transport and storage. Upon immobilization on a conductive surface, heme proteins can accomplish bioelectrocatalysis. In this process, they carry out oxidation or reduction of substrates at a solid electrode acting as electron acceptor or donor, respectively, thanks to electron transfer processes occurring at the interphase. The efficiency of bioelectrocatalysis depends on the electrical communication of the protein with the electrode surface, retention of protein structure upon adsorption and accessibility of the substrate to the active site. This Minireview outlines the main factors affecting bioelectrocatalysis by adsorbed heme proteins, highlights open issues, and summarizes recent advances in the field.

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Section: Bioelectrocatalysismentioning

confidence: 99%

Section: Other Proteinsmentioning

confidence: 99%

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

et al. 2019

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“…The peak current of the reduction of H2O2 increases with increasing the concentration of H2O2 from 60 μM to 0.1 mM. For SiO2 NPs/cyt c/MUA/Au, upon addition of H2O2 into buffer solution, the corresponding reduction current exhibits a larger degree of increase compared with that of cyt c/MUA/Au, suggesting that the interaction of SiO2 NPs could strengthen the electrocatalytic activity of cyt c towards the reduction of H2O2[34,35], which might be caused by the conformational change of cyt c after interaction with SiO2 NPs[36].…”

mentioning

confidence: 80%

Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface

Zhang

Zeng

Liu

et al. 2016

Electrochimica Acta

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Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface, Electrochimica Acta http://dx. AbstractStudy of the interactions between engineered nanoparticles and biomolecules plays an important role in understanding nano-bio effect. However, most of studies focus on the interaction of protein with nanoparticle in bulk phase, the impact of nanoparticle on the function of protein immobilized on the biological interface has been ignored for a long time. In this paper, we study the effect of SiO2 NPs on electron transfer function of cytochrome c (cyt c) adsorbed onto the 11-mercaptoundecanoic acid (MUA) self-assembled monolayer (SAM) by surface-enhanced infrared absorption spectroscopy (SEIRAS) combined with electrochemistry. Our results disclose that instead of inhibiting the electron transfer, exposure of SiO2 NPs enhances the redox reversibility, electron transfer rate, and catalytic performance of adsorbed cyt c, but induces a slight negative shift in the formal potential of the adsorbed cyt c. Interaction of SiO2 NPs slightly induces the structural changes of the β-sheet in the oxidized form and the change of microenvironment surrounding them, which could further change the microenvironment and the orientation of heme, facilitating the hydration of cyt c at the oxidized state. It could be the enhanced hydration of cyt c (Fe 3+ ) and a smaller change in the total hydration from reduced to oxidized state that results in the slight negative shift in the formal potential and promotes the electron transfer capability. Besides, cyt c's slight conformational change and the disturbance to the microenvironment of heme resulting from the adsorption of SiO2 NPs could also be one of the reason that leads to the enhanced catalytic capability towards the reduction of H2O2.

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“…[16,29,55] Indeed, cyclic voltammograms recorded at different scan rates and in a wider potential window (from -0.6 to +0.7 V) showed that the immobilized cytochrome-c is not denatured because of the absence of an additional reduction peak at more negative potential ( Figure S3). [16][17][18]22] A slight desorption of the immobilized protein could be observed after ten potential cycles between +0.3 V and -0.2 V, which led to about a 10% decrease of the redox signal ( Figure S4B). [16][17][18] This indicates a better stability of the immobilized cytochrome-c at the glassy carbon electrode modified with a small amount of cardiolipin (7 μg cm -2 ) in comparison with a previous study with a high cardiolipin lipid loading at the electrode (~700 μg cm -2 ).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…[2] The specific and selective interaction between cardiolipin and cytochrome-c is not well understood and has been assigned to a combination of electrostatic and hydrophobic effects, hydrogen bonding and/or the formation of a cardiolipin/cytochrome-c complex. [2,[6][7][8][9][10][11][12][15][16][17][18] The electrochemical behavior of redox proteins such as cytochrome-c, a water-soluble haemoprotein involved in the respiratory chain of mitochondria, has been extensively reported since 1977. [19][20][21][22] This model redox protein has often been studied at lipid-modified electrodes because the detection of its electroactivity is seldom possible at bare electrode surfaces even with large scanning potential range.…”

Section: Introductionmentioning

confidence: 99%

An optimal surface concentration of pure cardiolipin deposited onto glassy carbon electrode promoting the direct electron transfer of cytochrome-c

Lebègue

Smida

Flinois

et al. 2018

Journal of Electroanalytical Chemistry

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Pure cardiolipin deposit onto electrodes is optimized and shown to yield an efficient supported lipid film for promoting cytochrome-c immobilization and electroactivity. Cyclic voltammetry and electrochemical impedance spectroscopy measurements in an aqueous electrolyte with potassium ferri-and ferrocyanide as a redox probe evidence that an optimized pure cardiolipin film is reached for a 7 μg cm-2 deposit onto glassy carbon electrode. At this optimized surface concentration the pure cardiolipin deposit yields the most compact and less permeable supported lipid film on electrode surface. The thickness and the organization of the pure cardiolipin films were analyzed by atomic force microscopy (AFM) measurements. AFM imaging in aqueous buffer shows that the lipid deposit onto the surface forms a thick deposit of approximately 30 ± 10 nm of height with 4 nm average roughness and includes

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Thermodynamics and kinetics of reduction and species conversion at a hydrophobic surface for mitochondrial cytochromes c and their cardiolipin adducts

Cited by 16 publications

References 64 publications

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface

An optimal surface concentration of pure cardiolipin deposited onto glassy carbon electrode promoting the direct electron transfer of cytochrome-c

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