Electrostatic effects on the kinetics of oxidation-reduction reactions of c-type cytochromes.

Goldkorn, Tzipora; Schejter, Abel

doi:10.1016/s0021-9258(19)86351-2

Cited by 48 publications

(15 citation statements)

References 21 publications

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“…There have been a number of studies of the effect of ionic strength on the rates of electron transfer between metalloproteins and metal complexes [159][160][161][162][163][164][165][166][167]. The charges on the reactants are varied in these studies by using metal complexes of different charge types and/or by varying the charges on the protein through pH variations or by modifying the protein.…”

Section: Ivd Work Terms For Bimolecular Reactions Involving Metalloproteinsmentioning

confidence: 99%

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Electron transfers in chemistry and biology

Marcus

Sutin

1985

Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics

8,297

230

7,865

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Section: Ivd Work Terms For Bimolecular Reactions Involving Metalloproteinsmentioning

confidence: 99%

“…In using Eqn. 38 simplifying assumptions for o I and o 2 are often made: (i) o12 = ol + 02 with o~ = a~ + 0.15 nm [172] or (ii) o12 = o 1 + o 2 with o~ = a~ [163,[169][170][171]. The results obtained upon fitting the kinetic data to Eqn.…”

Section: Ivd Work Terms For Bimolecular Reactions Involving Metalloproteinsmentioning

confidence: 99%

Electron transfers in chemistry and biology

Marcus

Sutin

1985

Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics

8,297

230

7,865

View full text Add to dashboard Cite

show abstract

“…High ionic strength environments strongly alter the electrostatic interactions of all charged particles, such as ions, molecules, polyelectrolytes, and colloids, which can be utilized to improve both the selectivity and yield of catalytic reactions. − The dependence of reaction rates and Gibbs free energies on local electrical fields is exploited in electrocatalysis by varying the voltage applied to the electrode; however, in theory, the same effect can be harnessed without an external power source by varying the ionic strength of the media using compression of the double electric layers. High salt conditions have been used in electrocatalysis but not in other catalytic processes. ,, For example, high concentrations of electrolytes are known to lower activation barriers and increase yields in electrocatalytic CO 2 reduction, C–C coupling, and phenol oxidation .…”

Section: Introductionmentioning

confidence: 99%

Photocatalytic Hedgehog Particles for High Ionic Strength Environments

et al. 2021

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High ionic strength environments can profoundly influence catalytic reactions involving charged species. However, control of selectivity and yield of heterogeneous catalytic reactions involving nano- and microscale colloids remains hypothetical because high ionic strength leads to aggregation of particle dispersions. Here we show that microscale hedgehog particles (HPs) with semiconductor nanoscale spikes display enhanced stability in solutions of monovalent/divalent salts in both aqueous and hydrophobic media. HPs enable tuning of photocatalytic reactions toward high-value products by adding concentrated inert salts to amplify local electrical fields in agreement with Derjaguin, Landau, Verwey, and Overbeek theory. After optimization of HP geometry for a model photocatalytic reaction, we show that high salt conditions increase the yield of HP-facilitated photooxidation of 2-phenoxy-1-phenylethanol to benzaldehyde and 2-phenoxyacetophenone by 6 and 35 times, respectively. Depending on salinity, electrical fields at the HP–media interface increase from 1.7 × 104 V/m to 8.5 × 107 V/m, with high fields favoring products generated via intermediate cation radicals rather than neutral species. Electron transfer rates were modulated by varying the ionic strength, which affords a convenient and hardly used reaction pathway for engineering a multitude of redox reactions including those involved in the environmental remediation of briny and salty water.

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“…17,18,20 Several groups have analyzed the electrostatic interactions between proteins and charged ligands to yield effective charges of proteins by fitting eq 2 or eq 3 to experimental data. 1,9,11,13,14 The concept of effective charge is helpful to determine how charged ligands feel the charge of the protein in solution. In addition, this method can be applied to structurally unidentified proteins.…”

Section: Introductionmentioning

confidence: 99%

“…The charge of an individual amino acid side chain depends on the solution conditions such as pH and ionic strength ( I ). Therefore, to understand the electrostatic interactions, the dependence of the protein–protein or protein–ligand bimolecular rate constants ( k ) or binding constants on I has been frequently investigated. − However, the charge distributions in proteins are complicated, making it difficult to analyze all of the electrostatic interactions. Therefore, proteins are frequently considered as ions with simple charges, and the experimental dependence of k on I is often explained by applying Debye–Hückel (DH) theory and transition state theory to protein systems.…”

Section: Introductionmentioning

confidence: 99%

Understanding of the Effects of Ionic Strength on the Bimolecular Rate Constant between Structurally Identified Redox Enzymes and Charged Substrates Using Numerical Simulations on the Basis of the Poisson–Boltzmann Equation

et al. 2016

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To understand electrostatic interactions in biomolecules, the bimolecular rate constants (k) between redox enzymes and charged substrates (in this study, redox mediators in the electrode reaction) were evaluated at various ionic strengths (I) for the mediated bioelectrocatalytic reaction. The k value between bilirubin oxidase (BOD) and positively charged mediators increased with I, while that between BOD and negatively charged mediators decreased with I. The opposite trend was observed for the reaction of glucose oxidase (GOD). In the case of noncharged mediators, the k value was independent of I for both BOD and GOD. These results reflect the electrostatic interactions between the enzymes and the mediators. Furthermore, we estimated k/k° (k° being the thermodynamic rate constant) by numerical simulation (finite element method) based on the Poisson-Boltzmann (PB) equation. By considering the charges of individual atoms involved in the amino acids around the substrate binding sites in the enzymes, the simulated k/k° values well reproduced the experimental data. In conclusion, k/k° can be predicted by PB-based simulation as long as the crystal structure of the enzyme and the substrate binding site are known.

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Electrostatic effects on the kinetics of oxidation-reduction reactions of c-type cytochromes.

Cited by 48 publications

References 21 publications

Electron transfers in chemistry and biology

Electron transfers in chemistry and biology

Photocatalytic Hedgehog Particles for High Ionic Strength Environments

Understanding of the Effects of Ionic Strength on the Bimolecular Rate Constant between Structurally Identified Redox Enzymes and Charged Substrates Using Numerical Simulations on the Basis of the Poisson–Boltzmann Equation

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