Thermodynamics Of Electron Transfer Research Articles

Quenching of reactive species by Avenanthramides: theoretical insight to the thermodynamics of electron transfer

Quenching of reactive species by Avenanthramides: theoretical insight to the thermodynamics of electron transfer

Intramolecular Hydrogen Bonding Effect on the Electron-Transfer Thermodynamics of a Series of o-Nitrobenzyl Alcohol Derivatives.

From thermoelectrochemical experiments and electronic structure calculations of a series of nitrobenzyl alcohol derivatives, the effect of intramolecular hydrogen bonding (IHB) on the electron transfer thermodynamics is discussed on a molecular basis. A linear correlation between formal reduction potential (E1/2) values and temperature was obtained for the temperature range from 300 to 350 K. Estimated electron transfer entropy values (ΔS)─determined from this dependence─and the enthalpy (ΔΔH) changes relative to o-nitrobenzyl alcohol confirmed that the effect of the formation of IHB proved to be decisive in the charge-transfer thermodynamics. The possibility of intermolecular hydrogen bonding is further discussed upon comparing thermodynamic data among three different solvents.

Correlation between Electronic Descriptor and Proton-Coupled Electron Transfer Thermodynamics in Doped Graphite-Conjugated Catalysts.

Graphite-conjugated catalysts (GCCs) provide a powerful framework for investigating correlations between electronic structure features and chemical reactivity of single-site heterogeneous catalysts. GCC-phenazine undergoes proton-coupled electron transfer (PCET) involving protonation of phenazine at its two nitrogen atoms with the addition of two electrons. Herein, this PCET reaction is investigated in the presence of defects, such as heteroatom dopants, in the graphitic surface. The proton-coupled redox potentials, EPCET, are computed using a constant potential periodic density functional theory (DFT) strategy. The electronic states directly involved in PCET for GCC-phenazine exhibit the same nitrogen orbital character as those for molecular phenazine. The energy εLUS of this phenazine-related lowest unoccupied electronic state in GCC-phenazine is identified as a descriptor for changes in PCET thermodynamics. Importantly, εLUS is obtained from only a single DFT calculation but can predict EPCET, which requires many such calculations. Similar electronic features may be useful descriptors for thermodynamic properties of other single-site catalysts.

Integration of a Random‐Rapid‐Equilibrium Binding Model of NOX2 Assembly with a Five‐State Rate‐Limiting Model of NOX2 Electron Flow facilitating Superoxide Production

Introduction Reactive oxygen species (ROS, e.g. O2.-, H2O2) play a crucial role in key physiological processes, including cell signaling. However, ROS overproduction leads to oxidative stress, which plays a critical role in cell injury/death and pathogenesis of many diseases. Mitochondria and members of the NADPH oxidase family are major sources of ROS in most mammalian cells. NOX2, the most complex and widely expressed NOX isoform, is the focus of the present study. NOX2 produces ROS, specifically, superoxide (O2.-), upon assembly of its membrane-bound subunits gp91phox and p22phox with the activated cytosolic subunits p40phox, p47phox, p67phox, and Rac. Upon NOX2 assembly and activation, electrons are transferred from substrate NADPH to molecular O2 through different redox centers of NOX2 complex, which is further regulated by pH, resulting in NADP+ and O2.-. Despite this knowledge, there is a lack of a quantitative and integrative understanding of the kinetics and regulation of NOX2 assembly and activation, electron flow, and ROS production. Method We propose four rate-limiting mechanisms for electron transfer from NADPH to O2 via NOX2 complex redox centers: 1) a five-state model with sequential electron transfer, 2) a five-state model with ping-pong electron transfer, 3) a three-state model with sequential electron transfer and full cooperativity, and 4) a three-state model with sequential electron transfer and no cooperativity. These models, which also account for pH regulation, were evaluated by fitting each to relevant experimental data. Model 1, which best described the data, was then integrated with our recent model of NOX2 assembly and activation which incorporates our hypothesized random-rapid-equilibrium binding mechanism for NOX2 assembly, regulations by guanine nucleotides (GTP, GDP), and mutual binding enhancements between individual cytosolic subunits (p40phox, p47phox, p67phox, Rac). Overall, the integrated model of NOX2 kinetics considers the thermodynamics of electron transfer through the five redox centers, biphasic inhibition by pH, assembly of cytosolic and membrane subunits, regulations by GTP and GDP, and mutual binding enhancements. Results The results of the model analysis showed that the transfer of electrons from NADPH to O2 is best described by the rate-limiting sequential electron transfer mechanism and that pH has a biphasic inhibitory effect on NOX2 reaction flux. Also, NOX2 is differentially activated and regulated by p40phox, p47phox, p67phox, and Rac subunits. The resulting integrated model can be used to quantify enhancements in the binding affinities of p47phox, p67phox and Rac subunitsby GTP, reductions in the binding affinities of the same cytosolic subunits by GDP, mutual binding enhancements between p40phox, p47phox, p67phox and Rac subunits. Conclusion We have developed and validated an integrated model of NOX2 assembly and activation, electron flow, and ROS production. The model serves as a mechanistic and quantitative framework for investigating the role of cell membrane NOX2-mediated ROS production in regulating diverse cellular mechanisms under physiological and pathophysiological conditions.

Electrode Materials in Modern Organic Electrochemistry

AbstractThe choice of electrode material is critical for achieving optimal yields and selectivity in synthetic organic electrochemistry. The material imparts significant influence on the kinetics and thermodynamics of electron transfer, and frequently defines the success or failure of a transformation. Electrode processes are complex and so the choice of a material is often empirical and the underlying mechanisms and rationale for success are unknown. In this review, we aim to highlight recent instances of electrode choice where rationale is offered, which should aid future reaction development.

Electrode Materials in Modern Organic Electrochemistry.

The choice of electrode material is critical for achieving optimal yields and selectivity in synthetic organic electrochemistry. The material imparts significant influence on the kinetics and thermodynamics of electron transfer, and frequently defines the success or failure of a transformation. Electrode processes are complex and so the choice of a material is often empirical and the underlying mechanisms and rationale for success are unknown. In this review, we aim to highlight recent instances of electrode choice where rationale is offered, which should aid future reaction development.

Impact of Iron–Sulfur Clusters on the Spin–Lattice Relaxation Rate and ESEEM Frequency of the Oxidized Primary Donor P700+· and Reduced Phylloquinone Acceptor A1−· in Radical Pairs in Photosystem I Embedded in Trehalose Glassy Matrix

ESEEM measurements were performed at two temperatures on Photosystem I (PS I) complexes depleted of the extrinsic PsaC subunit harboring iron–sulfur 4Fe–4S clusters FA/FB (abbreviated FX-core complexes) embedded in trehalose glassy matrix. The ESEEM modulation frequencies obtained for the FX-core complexes in trehalose matrix were similar at 150 K and 290 K. They correspond to a distance ~ 25 A between the oxidized primary donor P700·+ and reduced phylloquinone acceptor A1·−. This distance corresponds to the preferential charge separation pathway between P700·+ and A1B·− in the B-branch of the PS I redox cofactors, while the distance estimated previously for the intact PS I complexes (containing the extrinsic PsaC subunit) embedded in dry trehalose matrix was ~ 26 A, which is typical for the formation of P700·+A1A·− charge-separated radical pairs in the symmetrical A-branch (Sukhanov et al. in Appl Magn Reson 49:1011, 2018). The redirection of electron transfer preferentially from the A to the B-branch of redox cofactors observed in FX-core complexes embedded in dry trehalose matrix can be rationalized by the alteration of the protein domain rigidity/flexibility around phylloquinone molecules in the A1A and A1B sites, which affects the thermodynamics of electron transfer between P700 and A1 in the symmetrical branches of cofactors. This finding of similar modulation frequencies measured for FX-core complexes in trehalose matrix at 150 K and 290 K is opposite to our previously obtained results for intact PS I, where the value of ESEEM modulation frequency markedly decreased upon heating the sample from cryogenic to room temperature (Sukhanov et al. in Appl Magn Reson 49: 1011, 2018). Our comparison of FX-core complexes with intact PS I complexes suggests that 4Fe-4S clusters accelerate spin–lattice relaxation of the unpaired electron spins on the phylloquinone in the A1-site. The result serves as additional argument in favor of the molecular model of the cryoprotective effect of trehalose matrix on the functioning of PS I by way of rigidity changes of the hydrogen-bonding network of the protein with the matrix that is based on the Le Chatelier–Braun principle. According to this thermodynamic principle, changes in both rigidity and flexibility are compensated to establish new thermodynamic equilibria with restored global balance of rigidity and flexibility that is typical within functioning protein complexes.

Active Role of the Buffer in the Proton-Coupled Electron Transfer of Immobilized Iron Porphyrins.

Evaluation of the proton-coupled electron transfer thermodynamics of immobilized hemin is challenging due to the disparity of its electrochemical titration curves reported in the literature. Deviations from the one-electron, one-proton transfer at circumneutral pHs have been commonly ascribed to either the formation of dimeric species or the ionization of a second iron-bound water molecule. Herein, however, we report on non-idealities in the more acidic region, whose onset and extent vary with the nature and concentration of the commonly used phosphate and acetate buffers. It is shown that these deviations originate in the ligand-exchange binding between the oxidized aquo-hemin complex and the anionic components of the buffer, so that they are restricted to the pH interval where these forms coexist. A stepwise approach was developed to quantify unambiguously the apparent and intrinsic binding equilibrium constants. The apparent binding equilibrium constant exhibits a peak-shaped pH dependence, whose maximum is located at approximately the midpoint between the pKa of the iron-bound water and the first pKa of the buffer, and its magnitude is greater for the phosphate than for the acetate buffer. But strikingly, the opposite trend was found for the magnitude of the intrinsic binding equilibrium constants determined from the apparent ones, due to the different relative locations of the phosphoric and acetic pKa values with respect to that of the oxidized aquo-hemin. To probe the role of the heme propionic residues, a similar study was carried out with a propionic-free iron porphyrin containing eight ethyl residues. These substituents decrease the acidity of the iron-bound water, strengthen the iron(III)-acetate binding, weaken the iron(III)-dihydrogen phosphate binding, and enable the binding between iron(III) and monohydrogen phosphate, which was hampered in hemin by the presence of the negatively charged propionate residues. Overall, this work provides a more complete speciation of immobilized iron porphyrins under acidic conditions than previously considered, showing the substitutional lability of the aqua ligand in the oxidized state of the iron center and the reluctance of its hydroxyl counterpart to anion exchange. Knowledge of these redox- and pH-dependent bindings with the buffer components is crucial for a rigorous quantification of the proton-coupled electron transfer and the electrocatalytic activity of iron porphyrins.

Integrated Computational Modeling of the Kinetics and Regulation of NADPH Oxidase 2 Assembly, Activation, Electron Flow, and Superoxide Production

IntroductionReactive oxygen species (ROS) play a crucial role in key physiological processes, including cell signaling. However, ROS overproduction leads to oxidative stress, which plays a critical role in cell injury/death and pathogenesis of many diseases, including cardiovascular disease. Members of the NADPH oxidase (NOX) family that comprise of membrane and cytosolic components are known to be the major non‐mitochondrial sources of ROS in most mammalian cells. NOX2 is the most complex, widely expressed, and well‐studied of the NOX isoforms. NOX2 is activated upon assembly of its membrane‐bound subunits gp91phox and p22phox with the cytosolic subunits p40phox, p47phox, p67phox, and Rac facilitating electron flow and ROS production. Specifically, upon NOX2 assembly and activation, electrons are transferred from substrate NADPH to molecular O2 through different redox centers of NOX2 complex (further regulated by pH) resulting in oxidized NADP+ and reduced O2−. (superoxide). Yet, there is a lack of mechanistic and quantitative understanding of the kinetics and regulation of NOX2 assembly and the relative contributions of NOX2 subunits towards NOX2 activation, electron flow, and ROS production.MethodWe developed an integrated computational model to quantitatively describe the kinetics and regulation of NOX2 assembly, activation, electron flow, and ROS production. The model incorporates our hypothesized “random rapid equilibrium binding mechanism” for NOX2 assembly and activation, regulations by guanine nucleotides (GTP, GDP), and mutual binding enhancements between individual cytosolic subunits (p40phox, p47phox, p67phox, Rac). The model also considers the thermodynamics of electron transfer through different redox centers of NOX2 complex and biphasic inhibition by pH. The model uses diverse published experimental data to modularly estimate the unknown model parameters using the built‐in “fmincon” optimization algorithm in MATLAB.ResultsThe modeling and analysis show that NOX2 is differentially activated and regulated by p40phox, p47phox, p67phox, and Rac subunits. In addition, the assembly of NOX2 subunits is regulated by GTP, GDP, and other cytosolic subunits. The model can quantify enhancements in the binding affinities of p47phox, p67phox and Rac subunits by GTP, reductions in the binding affinities of the same cytosolic subunits by GDP, mutual binding enhancement between p47phox, p67phox and Rac subunits, and enhancement in the binding affinity of p47phox by p40phox. The model can also quantify the binding affinities of NADPH and O2 for NOX2 complex and the maximal NOX2 activities as functions of pH.ConclusionThe proposed model provides a quantitative and integrated understanding of the kinetics and regulation of NOX2 assembly, activation, and the importance of these processes in facilitating electron transfer and ROS production under different conditions. The model also serves as a mechanistic and quantitative framework for investigating the critical role of NOX2 complex‐mediated ROS production in regulating diverse cellular mechanisms under physiological and pathophysiological conditions.Support or Funding InformationNIH P01‐GM066730, P01‐HL116264, U01‐HL122199

A thermodynamically-constrained mathematical model for the kinetics and regulation of NADPH oxidase 2 complex-mediated electron transfer and superoxide production

Reactive oxygen species (ROS) play an important role in cell signaling, growth, and immunity. However, when produced in excess, they are toxic to the cell and lead to premature aging and a myriad of pathologies, including cardiovascular and renal diseases. A major source of ROS in many cells is the family of NADPH oxidase (NOX), comprising of membrane and cytosolic components. NOX2 is among the most widely expressed and well-studied NOX isoform. Although details on the NOX2 structure, its assembly and activation, and ROS production are well elucidated experimentally, there is a lack of a quantitative and integrative understanding of the kinetics of NOX2 complex, and the various factors such as pH, inhibitory drugs, and temperature that regulate the activity of this oxidase. To this end, we have developed here a thermodynamically-constrained mathematical model for the kinetics and regulation of NOX2 complex based on diverse published experimental data on the NOX2 complex function in cell-free and cell-based assay systems. The model incorporates (i) thermodynamics of electron transfer from NADPH to O2 through different redox centers of the NOX2 complex, (ii) dependence of the NOX2 complex activity upon pH and temperature variations, and (iii) distinct inhibitory effects of different drugs on the NOX2 complex activity. The model provides the first quantitative and integrated understanding of the kinetics and regulation of NOX2 complex, enabling simulation of diverse experimental data. The model also provides several novel insights into the NOX2 complex function, including alkaline pH-dependent inhibition of the NOX2 complex activity by its reaction product NADP+. The model provides a mechanistic framework for investigating the critical role of NOX2 complex in ROS production and its regulation of diverse cellular functions in health and disease. Specifically, the model enables examining the effects of specific targeting of various enzymatic sources of pathological ROS which could overcome the limitations of pharmacological efforts aimed at scavenging ROS which has resulted in poor outcomes of antioxidant therapies in clinical studies.

Thermodynamics of Proton and Electron Transfer in Tetranuclear Clusters with Mn-OH2/OH Motifs Relevant to H2O Activation by the Oxygen Evolving Complex in Photosystem II.

We report the synthesis of site-differentiated heterometallic clusters with three Fe centers and a single Mn site that binds water and hydroxide in multiple cluster oxidation states. Deprotonation of FeIII/II3MnII-OH2 clusters leads to internal reorganization resulting in formal oxidation at Mn to generate FeIII/II3MnIII-OH. 57Fe Mössbauer spectroscopy reveals that oxidation state changes (three for FeIII/II3Mn-OH2 and four for FeIII/II3Mn-OH clusters) occur exclusively at the Fe centers; the Mn center is formally MnII when water is bound and MnIII when hydroxide is bound. Experimentally determined p Ka (17.4) of the [FeIII2FeIIMnII-OH2] cluster and the reduction potentials of the [Fe3Mn-OH2] and [Fe3Mn-OH] clusters were used to analyze the O-H bond dissociation enthalpies (BDEO-H) for multiple cluster oxidation states. BDEO-H increases from 69 to 78 and 85 kcal/mol for the [FeIIIFeII2MnII-OH2], [FeIII2FeIIMnII-OH2], and [FeIII3MnII-OH2] clusters, respectively. Further insight of the proton and electron transfer thermodynamics of the [Fe3Mn-OH x] system was obtained by constructing a potential-p Ka diagram; the shift in reduction potentials of the [Fe3Mn-OH x] clusters in the presence of different bases supports the BDEO-H values reported for the [Fe3Mn-OH2] clusters. A lower limit of the p Ka for the hydroxide ligand of the [Fe3Mn-OH] clusters was estimated for two oxidation states. These data suggest BDEO-H values for the [FeIII2FeIIMnIII-OH] and [FeIII3MnIII-OH] clusters are greater than 93 and 103 kcal/mol, which hints to the high reactivity expected of the resulting [Fe3Mn═O] in this and related multinuclear systems.

Protein crosslinking improves the thermal resistance of plastocyanin immobilized on a modified gold electrode

Increasing the thermal stability of immobilized proteins is a motivating goal for improving the performance of electrochemical biodevices. In this work, we propose the immobilization of crosslinked plastocyanin from the thermophilic cyanobacterium Phormidium laminosum by simultaneous incubation of a mixture of plastocyanin and the coupling reagents. The thermal stability of the so built covalently immobilized protein films has been assessed by cyclic voltammetry in the 0–90 °C temperature range and has been compared to that of physisorbed films. It is shown that the protein loss along a thermal cycle is significantly reduced in the case of the crosslinked films, whose redox properties remain unaltered along a cyclic heating-cooling thermal scan, and can withstand the contact with 70 °C solutions for four hours. Comparison of thermal unfolding curves obtained by circular dichroism spectroscopy of both free and crosslinked protein confirms the improved thermic resistance of the crosslinked plastocyanin. Notably, the electron transfer thermodynamics of physisorbed and crosslinked plastocyanin films are quite similar, suggesting that the formation of intra- and inter-protein amide bonds do not affect the integrity and functionality of the copper redox centers. UV–Vis absorption and circular dichroism measurements corroborate that protein crosslinking does not alter the coordination geometry of the metal center.

Control of Surface and Edge Oxidation on Phosphorene.

Phosphorene is emerging as an important two-dimensional semiconductor, but controlling the surface chemistry of phosphorene remains a significant challenge. Here, we show that controlled oxidation of phosphorene determines the composition and spatial distribution of the resulting oxide. We used X-ray photoemission spectroscopy to measure the binding energy shifts that accompany oxidation. We interpreted these spectra by calculating the binding energy shift for 24 likely bonding configurations, including phosphorus oxides and hydroxides located on the basal surface or edges of flakes. After brief exposure to high-purity oxygen or high-purity water vapor at room temperature, we observed phosphorus in the +1 and +2 oxidation states; longer exposures led to a large population of phosphorus in the +3 oxidation state. To provide insight into the spatial distribution of the oxide, transmission electron microscopy was performed at several stages during the oxidation. We found crucial differences between oxygen and water oxidants: while pure oxygen produced an oxide layer on the van der Waals surface, water oxidized the material at pre-existing defects such as edges or steps. We propose a mechanism based on the thermodynamics of electron transfer to interpret these observations. This work opens a route to functionalize the basal surface or edges of two-dimensional (2D) black phosphorus through site-selective chemical reactions and presents the opportunity to explore the synthesis of 2D phosphorene oxide by oxidation.

The Roles of Biofilm Conductivity and Donor Substrate Kinetics in a Mixed-Culture Biofilm Anode.

We experimentally assessed the kinetics and thermodynamics of electron transfer (ET) from the donor substrate (acetate) to the anode for a mixed-culture biofilm anode. We interpreted the results with a modified biofilm-conduction model consisting of three ET steps in series: (1) intracellular ET, (2) non-Ohmic extracellular ET (EET) from an outer membrane protein to an extracellular cofactor (EC), and (3) ET from the EC to the anode by Ohmic-conduction in the biofilm matrix. The steady-state current density was 0.82 ± 0.03 A/m2 in a miniature microbial electrochemical cell operated at fixed anode potential of -0.15 V versus the standard hydrogen electrode. Illumina 16S-rDNA and -rRNA sequences showed that the Geobacter genus was less than 30% of the community of the biofilm anode. Biofilm conductivity was high at 2.44 ± 0.42 mS/cm, indicating that the maximum current density could be as high as 270 A/m2 if only Ohmic-conduction EET was limiting. Due to the high biofilm conductivity, the maximum energy loss for Ohmic-conduction EET was negligible, 0.085 mV. The energy loss in the second ET step also was small, only 20 mV, and the potential for the EC involved in the second ET was -0.15 V, a value documenting that >99% of the EC was in the oxidized state. Monod kinetics for utilization of acetate were relatively slow, and at least 87% of the energy loss was in the intracellular step. Thus, intracellular ET was the main kinetic and thermodynamic bottleneck to ET from donor substrate to the anode for a highly conductive biofilm.

Activation of Electron-Deficient Quinones through Hydrogen-Bond-Donor-Coupled Electron Transfer.

Quinones are important organic oxidants in a variety of synthetic and biological contexts, and they are susceptible to activation towards electron transfer through hydrogen bonding. Whereas this effect of hydrogen bond donors (HBDs) has been observed for Lewis basic, weakly oxidizing quinones, comparable activation is not readily achieved when more reactive and synthetically useful electron-deficient quinones are used. We have successfully employed HBD-coupled electron transfer as a strategy to activate electron-deficient quinones. A systematic investigation of HBDs has led to the discovery that certain dicationic HBDs have an exceptionally large effect on the rate and thermodynamics of electron transfer. We further demonstrate that these HBDs can be used as catalysts in a quinone-mediated model synthetic transformation.

Activation of Electron‐Deficient Quinones through Hydrogen‐Bond‐Donor‐Coupled Electron Transfer

AbstractQuinones are important organic oxidants in a variety of synthetic and biological contexts, and they are susceptible to activation towards electron transfer through hydrogen bonding. Whereas this effect of hydrogen bond donors (HBDs) has been observed for Lewis basic, weakly oxidizing quinones, comparable activation is not readily achieved when more reactive and synthetically useful electron‐deficient quinones are used. We have successfully employed HBD‐coupled electron transfer as a strategy to activate electron‐deficient quinones. A systematic investigation of HBDs has led to the discovery that certain dicationic HBDs have an exceptionally large effect on the rate and thermodynamics of electron transfer. We further demonstrate that these HBDs can be used as catalysts in a quinone‐mediated model synthetic transformation.

Molecular Density Functional Theory: Application to Solvation and Electron-Transfer Thermodynamics in Polar Solvents

A molecular density functional theory of solvation is presented. The solvation properties of an arbitrary solute in a given solvent, both described by a molecular force field, can be obtained by minimization of a position- and orientation-dependent free-energy density functional. In the homogeneous reference fluid approximation, the unknown excess term of the functional can be approximated by the angular-dependent direct correlation function of the pure solvent. This function can be extracted from a preliminary MD simulation of the pure solvent by computing the angular-dependent pair distribution function and solving subsequently the molecular Ornstein-Zernike equation. The corresponding functional can then be minimized on a three-dimensional cubic grid for positions and a Gauss-Legendre angular grid for orientations to provide the solvation free energy of embedded molecules at the same time as the solvent three-dimensional microscopic structure. This functional minimization procedure is much more efficient than direct molecular dynamics simulations combined with thermodynamic integration schemes. The approach is shown to be also pertinent to the molecular-level determination of electron-transfer properties such as reaction free energy and reorganization energy. It is illustrated for molecular solvation and photochemical electron-transfer reactions in acetonitrile, a prototypical polar aprotic solvent.

Electroactive mixed culture derived biofilms in microbial bioelectrochemical systems: The role of pH on biofilm formation, performance and composition

The pH-value played a crucial role for the development and current production of anodic microbial electroactive biofilms. It was demonstrated that only a narrow pH-window, ranging from pH 6 to 9, was suitable for growth and operation of biofilms derived from pH-neutral wastewater. Any stronger deviation from pH neutral conditions led to a substantial decrease in the biofilm performance. Thus, average current densities of 151, 821 and 730μAcm−2 were measured for anode biofilms grown and operated at pH 6, 7 and 9 respectively. The microbial diversity of the anode chamber community during the biofilm selection process was studied using the low cost method flow-cytometry. Thereby, it was demonstrated that the pH value as well as the microbial inocula had an impact on the resulting anode community structure. As shown by cyclic voltammetry the electron transfer thermodynamics of the biofilms was strongly depending on the solution’s pH-value.

Using Quenching Kinetics and Thermodynamics of Amino-Fluorophores as Empirical Tools for Predicting Boronic Acid Sensors Suitable for Use in Physiological Conditions

A series of water-soluble 1-amino-naphthalenes and 2-amino-fluorenes are prepared. These serve as model fluorophores for measuring the thermodynamics and kinetics of fluorescence quenching with phenylboronic acids and aliphatic amines. Steady-state and time-resolved fluorescence quenching kinetics are investigated using the Stern–Volmer method. Diffusion limited quenching constants and exergonic thermodynamics of electron transfer are derived for the 5-amino-1-napthol and 2-aminofluorene derivatives with phenylboronic acid and/or an aliphatic imine. No quenching and endergonic thermodynamics or electron transfer are observed for 5-sulfonamide, 5-sulfonic acid, or 5-hydroxy-7-sulfonic acid aminonaphthalene derivatives. Boronic acid sensors synthesized from these aminofluorophores by reductive amination with 2-formylphenylboronic acid undergo fluorescence revival in the presence of saccharides only when the fluorophore demonstrates diffusion limited quenching kinetics and exergonic thermodynamics of electron transfer with the boronic acid or imine quenchers. Thus, these two properties are suitable empirical tools for predicting saccharide-induced fluorescence revival of boronic acid sensors.

Spin Crossover-Coupled Electron Transfer of [M(tacn)2]3+/2+Complexes (tacn = 1,4,7-Triazacyclononane; M = Cr, Mn, Fe, Co, Ni)

The role of spin state equilibria on the thermodynamics of electron transfer in [M(tacn)(2)](3+/2+) complexes (tacn = 1,4,7-triazacyclononane; M = Cr, Mn, Fe, Co, Ni) was examined using density functional theory at the B3LYP*/cc-pVTZ(-f) level coupled to a continuum solvation model to afford excellent agreement between computed and experimental redox properties. An intuitive explanation of the previously observed nonperiodic trend in reduction potentials, which display a sawtooth pattern along the first-row transition metal series, is offered utilizing a novel diagrammatic illustration of the relationship between spin state energetics and reduction potentials. This representation leads to a generalized proposal for analyzing and designing nearly isoenergetic spin states of transition metals in a given ligand environment. A new ligand specific parameter alpha that allows for quantifying the differential reduction potential as a function of the metal identity is introduced, and a novel protocol is presented that divides the ligand-metal interactions into primary and secondary characteristics, which we anticipate will be useful for rationally designing the electronics of transition metal complexes in general.