Fundamental Studies of Long- and Short-Range Electron Exchange Mechanisms between Electrodes and Proteins

Khoshtariya, Dimitri E.

doi:10.1007/978-1-4614-0347-0_2

Cited by 19 publications

(51 citation statements)

References 347 publications

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“…where Re is the electron transfer distance, Ro is the electron transfer distance at the closest approach of the redox-active couple to the electrode, and β is the decay parameter, normally of the order of ca. 1 Å -1 [69].…”

Section: Sam -Modified Electrodes and Immobilized Speciesmentioning

confidence: 99%

“…Standard heterogeneous pathways also have some obvious disadvantages. Noteworthy are the strong impact of the electrode/solution interfacial potential drop on the electron transfer process, especially in the free diffusion regime for which it complicates the over-all kinetic analysis [68,69]; and possible changes in the redox-active molecules upon adsorption to an electrode; in particular the adsorption of biomacromolecules, such as proteins, can lead to their inactivation [69].…”

Section: Mechanisms Of Electron Exchange Between Electrode and Proteinmentioning

confidence: 99%

“…The chemical and physical properties of these films can be modified to provide additional control over the electron transfer. These include the variation of the chemical identity and composition (mixing/dilution) of the SAM terminal groups that are presented to the solution (electrolyte); e.g., they can be manipulated to control the binding position and orientation of biomolecules [69].…”

Section: Mechanisms Of Electron Exchange Between Electrode and Proteinmentioning

confidence: 99%

“…This difference could cause more variation in the effective charge-transfer distance, as compared to the ideal case with impermeable SAMs. Moreover, it can be suppose that, the SAM defects can be roughly classified as static and dynamic ones, ascribing the former to different kinds of pinholes and collapsed sites, whereas the latter corresponds to increased mobility, and may or may not be associated with particular structural defects [69].…”

Section: +/2+mentioning

confidence: 99%

“…These new developments identify a need to generalize modern charge transfer theory and bear on the use of electrochemical methods in modern bioengineering and biomedical applications [79]. Even the very first applications of SAMbased electrochemical systems enabled fundamental testing of basic features of contemporary charge transfer theory [69].…”

Section: Sam -Modified Electrodes and Immobilized Speciesmentioning

confidence: 99%

See 4 more Smart Citations

Modern Electrochemistry in Nanobiology and Sensorics

Sołoducho¹,

Cabaj²

2014

Modern Electrochemical Methods in Nano, Surface and Corrosion Science

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Section: Sam -Modified Electrodes and Immobilized Speciesmentioning

confidence: 99%

Section: Mechanisms Of Electron Exchange Between Electrode and Proteinmentioning

confidence: 99%

Section: Mechanisms Of Electron Exchange Between Electrode and Proteinmentioning

confidence: 99%

Section: +/2+mentioning

confidence: 99%

Section: Sam -Modified Electrodes and Immobilized Speciesmentioning

confidence: 99%

See 3 more Smart Citations

Modern Electrochemistry in Nanobiology and Sensorics

Sołoducho¹,

Cabaj²

2014

Modern Electrochemical Methods in Nano, Surface and Corrosion Science

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Forty years of theory-inspired experiments on charge-transfer via solutions and electrodes: the Georgian accents

Khoshtariya

Dolidze²,

Laliashvili

et al. 2023

J Solid State Electrochem

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Theory of Protein Charge Transfer: Electron Transfer between Tryptophan Residue and Active Site of Azurin

Sarhangi

Matyushov

2022

J. Phys. Chem. B

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One reaction step in the conductivity relay of azurin, electron transfer between the Cu-based active site and the tryptophan residue, is studied theoretically and by classical molecular dynamics simulations. Oxidation of tryptophan results in electrowetting of this residue. This structural change makes the free energy surfaces of electron transfer nonparabolic as described by the Qmodel of electron transfer. We analyze the medium dynamical effect on protein electron transfer produced by coupled Stokes-shift dynamics and the dynamics of the donor−acceptor distance modulating electron tunneling. The equilibrium donor−acceptor distance falls in the plateau region of the rate constant, where it is determined by the protein−water dynamics, and the probability of electron tunneling does not affect the rate. The crossover distance found here puts most intraprotein electron-transfer reactions under the umbrella of dynamical control. The crossover between the medium-controlled and tunneling-controlled kinetics is combined with the effect of the protein−water medium on the activation barrier to formulate principles of tunability of protein-based charge-transfer chains. The main principle in optimizing the activation barrier is the departure from the Gaussian-Gibbsian statistics of fluctuations promoting activated transitions. This is achieved either by incomplete (nonergodic) sampling, breaking the link between the Stokes-shift and variance reorganization energies, or through wetting-induced structural changes of the enzyme's active site.

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Fundamental Studies of Long- and Short-Range Electron Exchange Mechanisms between Electrodes and Proteins

Cited by 19 publications

References 347 publications

Modern Electrochemistry in Nanobiology and Sensorics

Modern Electrochemistry in Nanobiology and Sensorics

Forty years of theory-inspired experiments on charge-transfer via solutions and electrodes: the Georgian accents

Theory of Protein Charge Transfer: Electron Transfer between Tryptophan Residue and Active Site of Azurin

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