Carboxylates as proton-accepting groups in concerted proton-electron transfers. Electrochemistry of the 2,5-dicarboxylate 1,4-hydrobenzoquinone/2,5-dicarboxy 1,4-benzoquinone couple

Concerted proton and electron transfers (CPET) currently attract considerable theoretical and experimental attention, notably in view of their likely involvement in many enzymatic reactions. The role of carboxylate groups as proton-accepting sites in CPET reactions is explored by means of a cyclic voltammetric investigation of the 2,5-dicarboxy 1,4-benzoquinone/2,5-dicarboxylate 1,4-hydrobenzoquinone couple in a nonaqueous medium. The presence of carboxylate groups ortho to the phenol groups induces the removal of an electron to be coupled with the transfer of the phenolic proton to a carboxylate oxygen. The kinetics of the electrochemical reaction and the observation of a significant hydrogen/deuterium kinetic isotope effect unambiguously indicate that electron transfer and proton transfer are concerted, thus providing an additional demonstration of the role of carboxylate groups as proton-accepting sites in concerted proton-electron transfer reactions.     

Concerted proton-electron transfers. Consistency between electrochemical kinetics and their homogeneous counterparts

The concerted proton-electron transfer (CPET) oxidation of phenol with water (in water) and hydrogen phosphate as proton acceptors provides a good example for testing the consistency of the electrochemical and homogeneous approaches to a reaction, the comprehension of which raises more mechanistic and kinetic challenges than that of a simple outer-sphere electron transfer. Comparison of the intrinsic kinetic characteristics (obtained at zero driving force of the CPET reaction) shows that consistency is indeed observed after a careful identification and quantitation of side factors (electrical work terms, image force effects). Water (in water) appears as a better intrinsic proton acceptor than hydrogen phosphate in both cases in terms of reorganization energy and pre-exponential factor, corroborating the mechanism by which electron transfer is concerted with Grotthus-type proton translocation in water. Detailed compared analysis of the approaches also revealed that modest but significant electric field effects may be at work in the electrochemical case. Comparison with phenoxide ion oxidation, taken as a reference outer-sphere electron transfer, points to a CPET precursor complex that possesses a precise spatial structure allowing the formation of one or several H-bonds as required by the occurrence of the CPET reaction, thus decreasing considerably the number of efficient collisions compared with those undergone by structureless spherical reactants.     

Electrochemical and homogeneous proton-coupled electron transfers: concerted pathways in the one-electron oxidation of a phenol coupled with an intramolecular amine-driven proton transfer

Proton-coupled electron transfers currently attract considerable attention in view of their likely involvement in many natural processes. Electrochemistry, through techniques such as cyclic voltammetry, is an efficient way of investigating the reaction mechanism of these reactions, and deciding whether proton and electron transfers are concerted or occur in a stepwise manner. The oxidation of an ortho-substituted 4,6-di (tert-butyl)-phenol in which the phenolic hydrogen atom is transferred during the reaction to the nitrogen atom of a nearby amine is taken as illustrative example. A careful analysis of the cyclic voltammetric responses obtained with this compound and its OD derivative allows, after estimation of the various thermodynamic parameters, ruling out the occurrence of the square scheme mechanism involving the proton-electron and electron-proton sequences. Simulation and comparison of the rate constant and H/D kinetic isotope effect with theoretical predictions show that the experimental value of the preexponential factor is ca. 1 order of magnitude larger than the theoretical value. Detailed calculations suggest that an electric field effect is responsible for this discrepancy.     

Concerted proton-electron transfer reactions in water. are the driving force and rate constant depending on pH when water acts as proton donor or acceptor?

The competition between stepwise and concerted (CPET) pathways in proton-coupled electron-transfer reactions in water is discussed on thermodynamic and kinetic bases. In the case where water is the proton acceptor, the CPET pathway may compete favorably with the stepwise pathway. The main parameter of the competition is pK of the oxidized form of the substrate being smaller or larger than 0. The driving force of the forward reaction is however independent of pH, despite the equilibrium redox potential of the proton-electron system being a function of pH. At high pH values, CPET reactions involving OH- as proton acceptor may likewise compete favorably with stepwise pathways. The overall reaction rate constant is an increasing function of pH, not because the driving force depends on pH but because OH- is a reactant. In buffered media, association of the substrate with the basic components of the buffer offers an alternative CPET route; the driving force comes closer to that offered by the pH-dependent equilibrium redox potential.     

Pyridine as proton acceptor in the concerted proton electron transfer oxidation of phenol

Taking pyridine as a prototypal example of biologically important nitrogen bases involved in proton-coupled electron transfers, it is shown with the example of the photochemically triggered oxidation of phenol by Ru(III)(bpy)(3) that this proton acceptor partakes in a concerted pathway whose kinetic characteristics can be extracted from the overall kinetic response. The treatment of these data, implemented by the results of a parallel study carried out in heavy water, allowed the determination of the intrinsic kinetic characteristics of this proton acceptor. Comparison of the reorganization energies and of the pre-exponential factors previously derived for hydrogen phosphate and water (in water) as proton acceptors suggests that, in the case of pyridine, the proton charge is delocalized over a primary shell of water molecules firmly bound to the pyridinium cation.     

Concerted proton-electron transfer in the oxidation of hydrogen-bonded phenols

Three phenols with pendant, hydrogen-bonded bases (HOAr-B) have been oxidized in MeCN with various one-electron oxidants. The bases are a primary amine (-CPh(2)NH(2)), an imidazole, and a pyridine. The product of chemical and quasi-reversible electrochemical oxidations in each case is the phenoxyl radical in which the phenolic proton has transferred to the base, (*)OAr-BH(+), a proton-coupled electron transfer (PCET) process. The redox potentials for these oxidations are lower than for other phenols, predominately from the driving force for proton movement. One-electron oxidation of the phenols occurs by a concerted proton-electron transfer (CPET) mechanism, based on thermochemical arguments, isotope effects, and DeltaDeltaG(++)/DeltaDeltaG degrees . The data rule out stepwise paths involving initial electron transfer to form the phenol radical cations [(*)(+)HOAr-B] or initial proton transfer to give the zwitterions [(-)OAr-BH(+)]. The rate constant for heterogeneous electron transfer from HOAr-NH(2) to a platinum electrode has been derived from electrochemical measurements. For oxidations of HOAr-NH(2), the dependence of the solution rate constants on driving force, on temperature, and on the nature of the oxidant, and the correspondence between the homogeneous and heterogeneous rate constants, are all consistent with the application of adiabatic Marcus theory. The CPET reorganization energies, lambda = 23-56 kcal mol(-)(1), are large in comparison with those for electron transfer reactions of aromatic compounds. The reactions are not highly non-adiabatic, based on minimum values of H(rp) derived from the temperature dependence of the rate constants. These are among the first detailed analyses of CPET reactions where the proton and electron move to different sites.     

Enzymatic catalysis and transfers in solution. I. Theory and computations, a unified view

The transfer of hydride, proton, or H atom between substrate and cofactor in enzymes has been extensively studied for many systems, both experimentally and computationally. A simple equation for the reaction rate, an analog of an equation obtained earlier for electron transfer rates, is obtained, but now containing an approximate analytic expression for the bond rupture-bond forming feature of these H transfers. A "symmetrization," of the potential energy surfaces is again introduced [R. A. Marcus, J. Chem. Phys. 43, 679 (1965); J. Phys. Chem. 72, 891 (1968)], together with Gaussian fluctuations of the remaining coordinates of the enzyme and solution needed for reaching the transition state. Combining the two expressions for the changes in the difference of the two bond lengths of the substrate-cofactor subsystem and in the fluctuation coordinates of the protein leading to the transition state, an expression is obtained for the free energy barrier. To this end a two-dimensional reaction space (m,n) is used that contains the relative coordinates of the H in the reactants, the heavy atoms to which it is bonded, and the protein/solution reorganization coordinate, all leading to the transition state. The resulting expression may serve to characterize in terms of specific parameters (two "reorganization" terms, thermodynamics, and work terms), experimental and computational data for different enzymes, and different cofactor-substrate systems. A related characterization was used for electron transfers. To isolate these factors from nuclear tunneling, when the H-tunneling effect is large, use of deuterium and tritium transfers is of course helpful, although tunneling has frequently and understandably dominated the discussions. A functional form is suggested for the dependence of the deuterium kinetic isotope effect (KIE) on DeltaG degrees and a different form for the 13C KIE. Pressure effects on deuterium and 13C KIEs are also discussed. Although formulated for a one-step transfer of a light particle in an enzyme, the results would also apply to single-step transfers of other atoms and groups in enzymes and in solution.     

Theoretical study of electron, proton, and proton-coupled electron transfer in iron bi-imidazoline complexes.

A comparative theoretical investigation of single electron transfer (ET), single proton transfer (PT), and proton-coupled electron transfer (PCET) reactions in iron bi-imidazoline complexes is presented. These calculations are motivated by experimental studies showing that the rates of ET and PCET are similar and are both slower than the rate of PT for these systems (Roth, J. P.; Lovel, S.; Mayer, J. M. J. Am. Chem. Soc. 2000, 122, 5486). The theoretical calculations are based on a multistate continuum theory, in which the solute is described by a multistate valence bond model, the transferring hydrogen nucleus is treated quantum mechanically, and the solvent is represented as a dielectric continuum. For electronically nonadiabatic electron transfer, the rate expressions for ET and PCET depend on the inner-sphere (solute) and outer-sphere (solvent) reorganization energies and on the electronic coupling, which is averaged over the reactant and product proton vibrational wave functions for PCET. The small overlap of the proton vibrational wave functions localized on opposite sides of the proton transfer interface decreases the coupling for PCET relative to ET. The theory accurately reproduces the experimentally measured rates and deuterium kinetic isotope effects for ET and PCET. The calculations indicate that the similarity of the rates for ET and PCET is due mainly to the compensation of the smaller outer-sphere solvent reorganization energy for PCET by the larger coupling for ET. The moderate kinetic isotope effect for PCET arises from the relatively short proton transfer distance. The PT reaction is found to be dominated by solute reorganization (with very small solvent reorganization energy) and to be electronically adiabatic, leading to a fundamentally different mechanism that accounts for the faster rate.     

Proton-coupled electron transfer in soybean lipoxygenase

The proton-coupled electron transfer reaction catalyzed by soybean lipoxygenase-1 is studied with a multistate continuum theory that represents the transferring hydrogen nucleus as a quantum mechanical wave function. The inner-sphere reorganization energy of the iron cofactor is calculated with density functional theory, and the outer-sphere reorganization energy of the protein is calculated with the frequency-resolved cavity model for conformations obtained with docking simulations. Both classical and quantum mechanical treatments of the proton donor-acceptor vibrational motion are presented. The temperature dependence of the calculated rates and kinetic isotope effects is in agreement with the experimental data. The weak temperature dependence of the rates is due to the relatively small free energy barrier arising from a balance between the reorganization energy and the reaction free energy. The unusually high deuterium kinetic isotope effect of 81 is due to the small overlap of the reactant and product proton vibrational wave functions and the dominance of the lowest energy reactant and product vibronic states in the tunneling process. The temperature dependence of the kinetic isotope effect is strongly influenced by the proton donor-acceptor distance with the dominant contribution to the overall rate. This dominant proton donor-acceptor distance is significantly smaller than the equilibrium donor-acceptor distance and is determined by a balance between the larger coupling and the smaller Boltzmann probability as the distance decreases. Thus, the proton donor-acceptor vibrational motion plays a vital role in decreasing the dominant donor-acceptor distance relative to its equilibrium value to facilitate the proton-coupled electron transfer reaction.     

Mechanisms for proton release during water oxidation in the S2 to S3 and S3 to S4 transitions in photosystem II

The new high-resolution X-ray structure of photosystem II has allowed more detailed studies than before of water oxidation at the oxygen evolving complex (OEC). In the present study the two final S-transitions of water oxidation are studied. The electron coupled proton transfers are followed from the center of the OEC to Asp61, which is considered as the start of the transfer chain through the protein to the lumenal side. It is found that the proton transfers occur in multiple steps. Structures of intermediates and energy diagrams are derived and compared to experimental observations. Since the new experimental structure of the OEC is very similar to the one suggested earlier by density functional calculations, the O-O bond formation step remains essentially the same as the one suggested five years ago. An interesting new result is that the barrier for proton transfer within the OEC actually competes with the O-O bond formation step of being rate-limiting.     

Adiabatic and non-adiabatic concerted proton-electron transfers. Temperature effects in the oxidation of intramolecularly hydrogen-bonded phenols

The one-electron electrochemical and homogeneous oxidations of two closely similar aminophenols that undergo a concerted proton-electron transfer reaction, in which the phenolic proton is transferred to the nitrogen atom in concert with electron transfer, are taken as examples to test procedures that allow the separate determination of the degree of adiabaticity and the reorganization energy of the reaction. The Marcus (or Marcus-Hush-Levich) formalism is applicable in both cases, but not necessarily in its adiabatic version. Linearization of the activation-driving force laws simplifies the treatment of the kinetic data, notably allowing the use of Arrhenius plots to treat the temperature dependence of the rate constant. A correct estimation of the adiabaticity and reorganization energy requires the determination of the variation of the driving force with temperature. Application of these procedures led to the conclusion that, unlike previous reports, the homogeneous reaction is non-adiabatic, with a transmission coefficient of the order of 0.005, and that the self-exchange reorganization energy is about 1 eV lower than previously estimated. With such systems, the intramolecular reorganization energy, although sizable, is in fact rather modest, being only slightly larger than that for the outer-sphere electron transfer that produced the cation radical. The electrochemical reaction is, in contrast, adiabatic, as revealed by the temperature dependence of its standard rate constant obtained from cyclic voltammetric experiments. This difference in behavior is deemed to derive from the effect of the strong electric field within which the electrochemical reaction takes place, stabilizing a zwitterionic form of the reactant (in which the proton has been transferred from oxygen to nitrogen). Taking this difference in adiabaticity into account, the magnitudes of the reorganization energies of the two reactions appear to be quite compatible with one another, as revealed by an analysis of the solvent and intramolecular contributions in both cases.     

H-bond relays in proton-coupled electron transfers. Oxidation of a phenol concerted with proton transport to a distal base through an OH relay

Four molecules comprising a phenol moiety and a distal pyridine base connected by an intermediary H-bonding and an H-bonded alcohol group have been synthesized and their electrochemistry has been investigated by means of cyclic voltammetry. The molecules differ by the substituent at the alcohol functional carbon and by methyl groups on the pyridine. The reaction follows a concerted proton-electron transfer pathway as confirmed by the observation of a significant H/D kinetic isotope effect in all four cases. The standard rate constants characterizing each of the four compounds are analyzed in terms of reorganization energy and pre-exponential factor. Intramolecular and solvent reorganization energies appear as practically constant in the series, in which a previously investigated aminophenol is included, whereas significantly different pre-exponential factors are observed. That the latter, which is a measure of the efficiency of proton tunneling concerted with electron transfer, be substantially smaller with the H-bond relay molecules than with the aminophenol is related to the fact that two protons are moved in the first case instead of one in the second. Within the H-bond relay molecules, the pre-exponential factor varies with the substituent present at the alcohol functional carbon in the order CF(3) > H > CH(3), presumably as the result of a fine tuning of the balance between the H-bond accepting and H-bond donating properties of the central OH group. The kinetic H/D kinetic isotope effect increases accordingly in the same order.     

Reactions associated with ionization in water: a direct ab initio dynamics study of ionization in (H2O)17

Quasiclassical ab initio simulations of the ionization dynamics in a (H(2)O)(17) cluster, the first water cluster that includes a fourfold coordinated (internally solvated) water molecule, have been carried out to obtain a detailed picture of the elementary processes and energy redistribution induced by ionization in a model of aqueous water. General features observable from the simulations are the following: (i) well within 100 fs following the ionization, one or more proton transfers are seen to take place from the "ionized molecule" to neighboring molecules and beyond, forming a hydronium ion and a hydroxyl radical; (ii) two water molecules close to the ionized water molecule play an important role in the reaction, in what we term a "reactive trimer." The reaction time is gated by the encounter of the ionized water molecule with these two neighboring molecules, and this occurs anytime between 10 and 50 fs after the ionization. The distances of approach between the ionized molecule and the neighboring molecules indeed display best the time characteristics of the transfer of a proton, and thus of the formation of a hydronium ion and a OH radical. These findings are consistent with those for smaller cyclic clusters, albeit the dynamics of the proton transfer displays more varieties in the larger cluster than in the small cyclic clusters. We used a partitioning scheme for the kinetic energy in the (H(2)O)(17) system that distinguishes between the reactive trimer and the surrounding "medium." The analysis of the simulations indicates that the kinetic energy of the surrounding medium increases markedly right after the event of ionization, a manifestation of the local heating of the medium. The increase in kinetic energy is consistent with a reorganization of the surrounding medium, electrostatically forced in a very short time by the water cation and in a longer time by the formation of the hydronium ion.     

Excited‐State Multiple Proton Transfer Depending on the Acidity and Basicity of Mediating Alcohols in 7‐Azaindole–(ROH)2 (R=H,CH3) Complexes: A Theoretical Study

Long‐range proton transfer plays an important role in many chemical and biological phenomena. It has recently been reported that the rate of excited‐state multiple proton transfer depends on the acidity and basicity of mediating alcohols in the H‐bonded wire. The excited‐state triple proton transfer in 7‐azaindole complexes through cyclic H‐bonded wires was theoretically studied to investigate rates depending on the mediating alcohols. This study showed that the acidity and basicity of alcohols collectively functioned to assist proton transfers depending on the paths; the proton transfers of protolytic and solvolytic paths were assisted by the pull‐behind effect and the push‐ahead effect, respectively. Both proton‐donating and accepting abilities of alcohols in the H‐bonded wire can accumulate to help proton transfer, and the strong acidity and basicity of the alcohols with relatively small structural changes in the wire have larger impacts on reducing the activation energies than those of alcohols that trigger proton transfer.     

Electrochemical proton relay at the single-molecule level

A scheme for the experimental study of single-proton transfer events, based on proton-coupled two-electron transfer between a proton donor and a proton acceptor molecule confined in the tunneling gap between two metal leads in electrolyte solution is suggested. Expressions for the electric current are derived and compared with formalism for electron tunneling through redox molecules. The scheme allows studying the kinetics of proton and hydrogen atom transfer as well as kinetic isotope effects at the single-molecule level under electrochemical potential control.     

C–H oxidation in fluorenyl benzoates does not proceed through a stepwise pathway: revisiting asynchronous proton-coupled electron transfer

2-Fluorenyl benzoates were recently shown to undergo C–H bond oxidation through intramolecular proton transfer coupled with electron transfer to an external oxidant. Kinetic analysis revealed unusual rate-driving force relationships. Our analysis indicated a mechanism of multi-site concerted proton–electron transfer (MS-CPET) for all of these reactions. More recently, an alternative interpretation of the kinetic data was proposed to explain the unusual rate-driving force relationships, invoking a crossover from CPET to a stepwise mechanism with an initial intramolecular proton transfer (PT) (Costentin, Savéant, Chem. Sci., 2020, 11, 1006). Here, we show that this proposed alternative pathway is untenable based on prior and new experimental assessments of the intramolecular PT equilibrium constant and rates. Measurement of the fluorenyl 9-C–H pK_a, H/D exchange experiments, and kinetic modelling with COPASI eliminate the possibility of a stepwise mechanism for C–H oxidation in the fluorenyl benzoate series. Implications for asynchronous (imbalanced) MS-CPET mechanisms are discussed with respect to classical Marcus theory and the quantum-mechanical treatment of concerted proton–electron transfer.

2-Fluorenyl benzoates were recently shown to undergo C–H bond oxidation through intramolecular proton transfer coupled with electron transfer to an external oxidant.     

Myoglobin as an efficient electrocatalyst for nitromethane reduction

Xenobiotic metabolizing heme enzymes are thought to take a crucial part in the activation of a variety of carcinogens, including nitro compounds, through catalytic electron-transfer reactions, especially under anaerobic conditions. Myoglobin (Mb), as a model heme enzyme, is found to act as an efficient electrocatalyst for the reduction of nitromethane in thin surfactant films on pyrolytic graphite electrodes. The electrocatalytic process is characterized by cyclic voltammetry. The Mb-Fe(II)-nitrosomethane complex, a possible intermediate in the catalysis, is characterized spectroscopically in the surfactant film on indium tin oxide electrodes. Bulk electrolysis indicates the formation of mainly methylhydroxylamine as an end aqueous product. A rationale for the catalysis invokes the highly reduced Fe(I) state of myoglobin in surfactant film; the latter engages in efficient inner-sphere electron transfers to the nitro compound coupled to proton transfers.     

Proton-coupled electron transfer in soybean lipoxygenase: dynamical behavior and temperature dependence of kinetic isotope effects

The dynamical behavior and the temperature dependence of the kinetic isotope effects (KIEs) are examined for the proton-coupled electron transfer reaction catalyzed by the enzyme soybean lipoxygenase. The calculations are based on a vibronically nonadiabatic formulation that includes the quantum mechanical effects of the active electrons and the transferring proton, as well as the motions of all atoms in the complete solvated enzyme system. The rate constant is represented by the time integral of a probability flux correlation function that depends on the vibronic coupling and on time correlation functions of the energy gap and the proton donor-acceptor mode, which can be calculated from classical molecular dynamics simulations of the entire system. The dynamical behavior of the probability flux correlation function is dominated by the equilibrium protein and solvent motions and is not significantly influenced by the proton donor-acceptor motion. The magnitude of the overall rate is strongly influenced by the proton donor-acceptor frequency, the vibronic coupling, and the protein/solvent reorganization energy. The calculations reproduce the experimentally observed magnitude and temperature dependence of the KIE for the soybean lipoxygenase reaction without fitting any parameters directly to the experimental kinetic data. The temperature dependence of the KIE is determined predominantly by the proton donor-acceptor frequency and the distance dependence of the vibronic couplings for hydrogen and deuterium. The ratio of the overlaps of the hydrogen and deuterium vibrational wavefunctions strongly impacts the magnitude of the KIE but does not significantly influence its temperature dependence. For this enzyme reaction, the large magnitude of the KIE arises mainly from the dominance of tunneling between the ground vibronic states and the relatively large ratio of the overlaps between the corresponding hydrogen and deuterium vibrational wavefunctions. The weak temperature dependence of the KIE is due in part to the dominance of the local component of the proton donor-acceptor motion.     

Dynamic NMR study of the mechanisms of double, triple, and quadruple proton and deuteron transfer in cyclic hydrogen bonded solids of pyrazole derivatives

Using dynamic solid state (15)N CPMAS NMR spectroscopy (CP = cross polarization, MAS = magic angle spinning), the kinetics of the degenerate intermolecular double and quadruple proton and deuteron transfers in the cyclic dimer of (15)N labeled polycrystalline 3,5-diphenyl-4-bromopyrazole (DPBrP) and in the cyclic tetramer of (15)N labeled polycrystalline 3,5-diphenylpyrazole (DPP) have been studied in a wide temperature range at different deuterium fractions in the mobile proton sites. Rate constants were measured on a millisecond time scale by line shape analysis of the doubly (15)N labeled compounds, and by magnetization transfer experiments on a second timescale of the singly (15)N labeled compounds in order to minimize the effects of proton-driven (15)N spin diffusion. For DPBrP the multiple kinetic HH/HD/DD isotope effects could be directly obtained. By contrast, four rate constants k(1) to k(4) were obtained for DPP at different deuterium fractions. Whereas k(1) corresponds to the rate constant k(HHHH) of the HHHH isotopolog, an appropriate kinetic reaction model was needed for the kinetic assignment of the other rate constants. Using the model described by Limbach, H. H.; Klein, O.; Lopez Del Amo, J. M.; Elguero, J. Z. Phys. Chem. 2004,218, 17, a concerted quadruple proton-transfer mechanism as well as a stepwise consecutive single transfer mechanism could be excluded. By contrast, using the kinetic assignment k(2) approximately k(3) approximately k(HHHD) approximately k(HDHD) and k(3) approximately k(HDDD) approximately k(DDDD), the results could be explained in terms of a two-step process involving a zwitterionic intermediate. In this mechanism, each reaction step involves the concerted transfer of two hydrons, giving rise to primary kinetic HH/HD/DD isotope effects, whereas the nontransferred hydrons only contribute small secondary effects, which are not resolved experimentally. By contrast, the multiple kinetic isotope effects of the double proton transfer in DPBrP and of the triple proton proton transfer in cyclic pyrazole trimers studied previously indicate concerted transfer processes. Thus, between n = 3 and 4 a switch of the reaction mechanism takes place. This switch is rationalized in terms of hydrogen bond compression effects associated with the multiple proton transfers. The Arrhenius curves of all processes are nonlinear and indicate tunneling processes at low temperatures. In a preliminary analysis, they are modeled in terms of the Bell-Limbach tunneling model.     

Step-wise proton-coupled electron transfer extended to aminobenzoquinone modified monolayers

The step-wise proton coupled electron transfer (SW-PCET) model has been expanded to describe instances where three protons are transferred with either one or two electrons. Expressions have been derived describing the pH dependence of the apparent formal potential, apparent standard rate constant, apparent transfer coefficient, and reaction pathway. The expressions can be applied to both Marcus density of states theory as well as Butler-Volmer kinetics depending on the assumptions made about the individual transfer coefficients. An example of 2e3H has been provided for an aminobenzoquinone monolayer system and experimental measurements have been compared to model predictions. Although the large reorganization energy of the benzoquinone system prevents differentiation between Butler-Volmer and Marcus DOS kinetic behaviour, results are consistent with the SW-PCET model. These results indicate how acid/base substituents on tethered organic molecules can participate in PCET even though they themselves are redox inactive.