scholarly journals Redox Potential Tuning of the Small Multicopper Oxidase from Streptomyces Coelicolor

2012 ◽  
Keyword(s):  
Redox Potential ◽  
Streptomyces Coelicolor ◽  
Multicopper Oxidase ◽  
Redox Potential Tuning

Redox Potential Tuning of Dimolybdenum Systems through Systematic Substitution by Guanidinate Ligands

2020 ◽  
Vol 59 (5) ◽  
pp. 3091-3101
Author(s):  
Nancy Rodríguez-López ◽  
Nathalie Metta ◽  
Alejandro J. Metta-Magana ◽  
Dino Villagrán
Keyword(s):  
Redox Potential ◽  
Redox Potential Tuning

Redox potential tuning by redox-inactive anions in copper(II) complexes of non-innocent o-aminophenol-based ligand containing benzoxazole: Learning from nature

Polyhedron ◽  
2017 ◽  
Vol 122 ◽  
pp. 219-227 ◽  
Author(s):  
Elham Safaei ◽  
Hadiseh Bahrami ◽  
Andrzej Wojtczak ◽  
Saman Alavi ◽  
Zvonko Jagličić
Keyword(s):  
Redox Potential ◽  
Redox Potential Tuning

scholarly journals Redox Potential Tuning of s-Tetrazine by Substitution of Electron-Withdrawing/Donating Groups for Organic Electrode Materials

Molecules ◽  
2021 ◽  
Vol 26 (4) ◽  
pp. 894
Author(s):  
Dong Joo Min ◽  
Kyunam Lee ◽  
Hyunji Park ◽  
Ji Eon Kwon ◽  
Soo Young Park
Keyword(s):  
Redox Potential ◽  
Electrode Materials ◽  
Redox Potentials ◽  
Hammett Constant ◽  
Heterogeneous Electron Transfer ◽  
Organic Electrode ◽  
Conventional Electrode ◽  
Li Ion ◽  
Cv Measurements ◽  
Redox Potential Tuning

Herein, we tune the redox potential of 3,6-diphenyl-1,2,4,5-tetrazine (DPT) by introducing various electron-donating/withdrawing groups (methoxy, t-butyl, H, F, and trifluoromethyl) into its two peripheral benzene rings for use as electrode material in a Li-ion cell. By both the theoretical DFT calculations and the practical cyclic voltammetry (CV) measurements, it is shown that the redox potentials (E1/2) of the 1,2,4,5-tetrazines (s-tetrazines) have a strong correlation with the Hammett constant of the substituents. In Li-ion coin cells, the discharge voltages of the s-tetrazine electrodes are successfully tuned depending on the electron-donating/withdrawing capabilities of the substituents. Furthermore, it is found that the heterogeneous electron transfer rate (k0) of the s-tetrazine molecules and Li-ion diffusivity (DLi) in the s-tetrazine electrodes are much faster than conventional electrode active materials.

Redox potential tuning in bio-relevant heterocycles via (anti)aromaticity modulated H-bonding (AMHB)

2020 ◽  
Vol 98 (7) ◽  
pp. 337-346
Author(s):  
Tayeb Kakeshpour ◽  
Adam Van Wiemeersch ◽  
James E. Jackson
Keyword(s):  
Redox Potential ◽  
Rational Design ◽  
Bond Formation ◽  
Complex Structures ◽  
Redox Potentials ◽  
Biologically Relevant ◽  
Connectivity Patterns ◽  
Non Covalent Interactions ◽  
Redox Potential Tuning ◽  
Covalent Interactions

Hydrogen bonds are arguably the most important non-covalent interactions in chemistry and biology, and their strength and directionality have been elegantly exploited in the rational design of complex structures. We recently noted that the variable responses of cyclic π-systems upon H-bond formation reciprocally lead to modulations of the H-bonds’ strengths, a phenomenon that we dubbed (anti)aromaticity-modulated hydrogen bonding (AMHB) [J. Am. Chem. Soc. 2016, 138, 3427–3432]. Species that switch from aromatic to antiaromatic or vice versa upon changing π-electron counts should be oppositely stabilized by the AMHB effects, so their redox potentials should be significantly “tuned” by H-bond formation. Herein, using quantum chemical simulations, we explore the effects of these H-bond induced π-electron polarizations on the redox potentials of (anti)aromatic heterocycles. The systems chosen for this study have embedded amide groups and amidine moieties capable of forming two-point H-bonds in their cyclic π-systems. Thus, as the 4-electron and 6-electron π-systems in redox-capable monocycles (e.g., quinones) can be differentially stabilized, their redox potentials can be modulated by H-bond formation by as much as 6 kcal/mol (258 mV for one electron transfer). In fused rings, the connectivity patterns are as important as the π-electron counts. Extending these ideas to flavin, a biologically relevant case, we find that H-bonding patterns like those found in its crystals can vary its redox potential by up to 1.3 kcal/mol.

scholarly journals Redox Potential Tuning through Differential Quinone Binding in the Photosynthetic Reaction Center of Rhodobacter sphaeroides

Biochemistry ◽  
2015 ◽  
Vol 54 (12) ◽  
pp. 2104-2116 ◽  
Author(s):  
Josh V. Vermaas ◽  
Alexander T. Taguchi ◽  
Sergei A. Dikanov ◽  
Colin A. Wraight ◽  
Emad Tajkhorshid
Keyword(s):  
Redox Potential ◽  
Reaction Center ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Reaction Center ◽  
Quinone Binding ◽  
Redox Potential Tuning

Redox potential tuning by redox-inactive cations in nature's water oxidizing catalyst and synthetic analogues

2016 ◽  
Vol 18 (16) ◽  
pp. 10739-10750 ◽  
Author(s):  
Vera Krewald ◽  
Frank Neese ◽  
Dimitrios A. Pantazis
Keyword(s):  
Redox Potential ◽  
Synthetic Analogues ◽  
Manganese Clusters ◽  
Biological Water ◽  
Redox Potential Tuning

Fundamental differences between synthetic manganese clusters and the biological water oxidizing catalyst are demonstrated in the modulation of their redox potential by redox-inactive cations.

scholarly journals Interference Reduction in Glucose Detection by Redox Potential Tuning: New Glucose Meter Development

2015 ◽  
Vol 31 (7) ◽  
pp. 705-710 ◽  
Author(s):  
Seong Je CHO ◽  
Chul-Ho CHO ◽  
Kwang Bok KIM ◽  
Min-Hyoung LEE ◽  
Jae Hong KIM ◽  
...  
Keyword(s):  
Redox Potential ◽  
Glucose Detection ◽  
Interference Reduction ◽  
Glucose Meter ◽  
Redox Potential Tuning

scholarly journals Significant improvement of oxidase activity through the genetic incorporation of a redox-active unnatural amino acid

2015 ◽  
Vol 6 (7) ◽  
pp. 3881-3885 ◽  
Author(s):  
Yang Yu ◽  
Qing Zhou ◽  
Li Wang ◽  
Xiaohong Liu ◽  
Wei Zhang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Redox Potential ◽  
Oxidase Activity ◽  
Unnatural Amino Acid ◽  
Redox Active ◽  
Redox Potential Tuning ◽  
Genetic Incorporation

Incorporation of 3-methoxytyrosine boosts the oxidase activity of the myoglobin model of oxidase, stressing the importance of the redox potential tuning of tyrosine.

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