Proton-coupled Electron Transfer Mechanism Research Articles

Photoredox-Catalyzed Oxidation of Anions for the Atom-Economical Hydro-, Amido-, and Dialkylation of Alkenes.

Photoredox catalysis has become a powerful method to generate free radical intermediates in organic synthesis. This report describes the use of photoredox catalysis to directly oxidize common nucleophilic anions to access electrophilic 1,3-dicarbonyl and amidyl radical intermediates. First, conjugate bases of 1,3-dicarbonyls were oxidized to neutral radical species for intramolecular hydro- and dialkylation of alkenes. This overall redox-neutral process provided cyclopentanone products in excellent yields (up to 96%). The scope included a variety of styrene radical acceptors and products with newly formed vicinal quaternary carbons. This process was then extended to the synthesis of pyrrolidinones by alkene amidoalkylation that proceeded via N-aryl amidyl radical intermediates in good yield (up to 85%). These reactions were characterized by their mild conditions, high atom economy, and the absence of stoichiometric byproducts. Mechanistic and computational studies supported a stepwise proton-coupled electron transfer mechanism, where an "electron borrowing" photocatalyst oxidizes an anion and reduces a benzylic radical after bond formation.

Structural and Thermodynamic Effects on the Kinetics of C-H Oxidation by Multisite Proton-Coupled Electron Transfer in Fluorenyl Benzoates.

Our recent experimental and theoretical investigations have shown that fluorene C-H bonds can be activated through a mechanism in which the proton and electron are transferred from the C-H bond to a separate base and oxidant in a concerted, elementary step. This multisite proton-coupled electron transfer (MS-PCET) mechanism for C-H bond activation was shown to be facilitated by shorter proton donor-acceptor distances. With the goal of intentionally modulating this donor-acceptor distance, we have now studied C-H MS-PCET in the 3-methyl-substituted fluorenyl benzoate (2-Flr-3-Me-BzO-). This derivative was readily oxidized by ferrocenium oxidants by initial C-H MS-PCET, with rate constants that were 6-21 times larger than those for 2-Flr-BzO- with the same oxidants. Structural comparisons by X-ray crystallography and by computations showed that addition of the 3-methyl group caused the expected steric compression; however, the relevant C···O- proton donor-acceptor distance was longer, due to a twist of the carboxylate group. The structural changes induced by the 3-Me group increased the basicity of the carboxylate, weakened the C-H bond, and reduced the reorganization energy for C-H bond cleavage. Thus, the rate enhancement for 2-Flr-3-Me-BzO- was due to effects on the thermochemistry and kinetic barrier, rather than from compression of the C···O- proton donor-acceptor distance. These results highlight both the challenges of controlling molecules on the 0.1 Å length scale and the variety of parameters that affect PCET rate constants.

Chemical repair of damaged leucine and tryptophane by thiophenols at close to diffusion-controlled rates: Mechanisms and kinetics.

Thiophenols are chemical species with multiple desirable biological properties, including their primary and secondary antioxidant capacity. In this work, the repairing antioxidant activity of eight different thiophenols has been investigated for damaged leucine and tryptophane. The investigation was carried out employing quantum mechanical and transition state methods to calculate the thermodynamic and kinetic data of the reactions involved, while simulating the biological conditions at physiological pH and aqueous and lipidic medium. The analysis of the atomic charges and the spin densities at each of the points on the potential energy surface was the tool that allowed the elucidation of the reaction mechanisms through which thiophenols repair the oxidative damage caused to the amino acids leucine and tryptophan. It was found that thiophenols can repair leucine via a hydrogen atom transfer mechanism in a manner which is similar to the one used by glutathione to repair the carbon-centered radicals of guanosine. In addition, thiophenols can also restore tryptophane, a nitrogen-centered radical, via proton-coupled electron transfer and single electron transfer mechanisms. Moreover, both processes occur at close to diffusion-controlled rates.

Multiple Proton-Coupled Electron Transfers at a Tricopper Cluster: Modeling the Reductive Regeneration Process in Multicopper Oxidases.

Metal clusters in enzymes carry out the life-sustaining reactions by accumulating multiple redox equivalents in a narrow potential range. This redox potential leveling effect commonly observed in Nature has yet to be reproduced with synthetic metal clusters. Herein, we employ a fully encapsulated synthetic tricopper complex to model the three-electron two-proton reductive regeneration of fully reduced trinuclear copper cluster CuICuICuI(μ2-OH2) (FR) from native intermediate CuIICuIICuII(μ3-O) (NI) in multicopper oxidases (MCOs). The tricopper cluster can access four oxidation states (I,I,I to II,II,II) and four protonation states ([Cu3(μ3-O)]LH, [Cu3(μ3-OH)]L, [Cu3(μ3-OH)]LH, and [Cu3(μ3-OH2)]L, where LH denotes the protonated ligand), allowing mechanistic investigation of proton-coupled electron transfer (PCET) relevant to MCOs. Seven tricopper complexes with discrete oxidation and protonation states were characterized with spectroscopy or X-ray single-crystal diffraction. A stepwise electron transfer-proton transfer (ET-PT) mechanism is established for the reduction of CuIICuIICuII(μ3-O)LH to CuIICuIICuI(μ3-OH)L, while a stepwise PT-ET mechanism is determined for the reduction of CuIICuICuI(μ3-OH)LH to CuICuICuI(μ2-OH2)L. The switch-over from ET-PT to PT-ET mechanism showcases that the tricopper complex can adopt different PCET mechanisms to circumvent high-barrier proton transfer steps. Overall, three-electron two-proton reduction occurs within a narrow potential range of 170 mV, exemplifying the redox potential leveling effect of secondary proton relays in delivering multiple redox equivalents at metal clusters.

Prussian blue analogues derived electrocatalyst with multicatalytic centers for boosting oxygen reduction reaction in the wide pH range

Due to the complex of oxygen reduction reaction (ORR), designing catalysts with multicatalytic centers is considered as a promising way for boosting the ORR. Herein, a multicatalytic centers electrocatalyst Fe3C/Mn3O4 encased by N-doped graphitic layers (FeMn PDA-900) is synthesized using iron manganese Prussian blue analogues and dopamine as the precursor. It exhibits a half-wave potential (E1/2) of 0.86 V for ORR and yields of H2O2 lower than 5% in 0.1 M KOH. Moreover, the prepared catalyst has also shown high catalytic ORR performance in both acidic and neutral electrolyte solutions, which exhibits the potential application in both the proton exchange membrane fuel cell and the microbial electrolysis cell. It is found that the good performance can be well explained by proton-coupled electron transfer mechanism due to the multicatalytic centers from Fe-Nx, Fe3C and Mn3O4 for providing enough active sites at the same time and the N-doped graphitic layers as a bridge for facilitating the electron transfer between the interfaces of Fe3C/Mn3O4 nanoparticles, which paves the way for protons and electrons transfer simultaneously and rapidly, and thus lowing the energy barrier and facilitating the ORR process. Therefore, FeMn PDA-900 is a promising candidate to replace precious metal-based ORR electrocatalysts at the whole pH range.

Electrochemical and Mechanistic Study of Reactivities of α-, β-, γ-, and δ-Tocopherol toward Electrogenerated Superoxide in N,N-Dimethylformamide through Proton-Coupled Electron Transfer

Scavenging of superoxide radical anion (O2•−) by tocopherols (TOH) and related compounds was investigated on the basis of cyclic voltammetry and in situ electrolytic electron spin resonance spectrum in N,N-dimethylformamide (DMF) with the aid of density functional theory (DFT) calculations. Quasi-reversible dioxygen/O2•− redox was modified by the presence of TOH, suggesting that the electrogenerated O2•− was scavenged by α-, β-, γ-TOH through proton-coupled electron transfer (PCET), but not by δ-TOH. The reactivities of α-, β-, γ-, and δ-TOH toward O2•− characterized by the methyl group on the 6-chromanol ring was experimentally confirmed, where the methyl group promotes the PCET mechanism. Furthermore, comparative analyses using some related compounds suggested that the para-oxygen-atom in the 6-chromanol ring is required for a successful electron transfer (ET) to O2•− through the PCET. The electrochemical and DFT results in dehydrated DMF suggested that the PCET mechanism involves the preceding proton transfer (PT) forming a hydroperoxyl radical, followed by a PCET (intermolecular ET–PT). The O2•− scavenging by TOH proceeds efficiently along the PCET mechanism involving one ET and two PTs.

The Ultrafast Quantum Dynamics of Photoexcited Adenine-Thymine Basepair Investigated with a Fragment-based Diabatization and a Linear Vibronic Coupling Model.

In this contribution we present a quantum dynamical study of the photoexcited hydrogen bonded base pair adenine–thymine (AT) in a Watson–Crick arrangement. To that end, we parametrize Linear Vibronic Coupling (LVC) models with Time-Dependent Density Functional Theory (TD-DFT) calculations, exploiting a fragment diabatization scheme (FrD) we have developed to define diabatic states on the basis of individual chromophores in a multichromophoric system. Wavepacket propagations were run with the multilayer extension of the Multiconfiguration Time-Dependent Hartree method. We considered excitations to the three lowest bright states, a ππ* state of thymine and two ππ* states (La and Lb) of adenine, and we found that on the 100 fs time scale the main decay pathways involve intramonomer population transfers toward nπ* states of the same nucleobase. In AT this transfer is less effective than in the isolated nucleobases, because hydrogen bonding destabilizes the nπ* states. The population transfer to the A → T charge transfer state is negligible, making the ultrafast (femtosecond) decay through the proton coupled electron transfer mechanism unlikely, in line with experimental results in apolar solvents. The excitation energy transfer is also very small. We carefully compare the predictions of LVC Hamiltonians obtained with different sets of diabatic states, defined so to match either local states of the two separated monomers or the base pair adiabatic states in the Franck–Condon region. To that end we also extend the flexibility of the FrD-LVC approach, introducing a new strategy to define fragments diabatic states that account for the effect of the rest of the multichromohoric system through a Molecular Mechanics potential.

Semiempirical method for examining asynchronicity in metal–oxido-mediated C–H bond activation

The oxidation of substrates via the cleavage of thermodynamically strong C-H bonds is an essential part of mammalian metabolism. These reactions are predominantly carried out by enzymes that produce high-valent metal-oxido species, which are directly responsible for cleaving the C-H bonds. While much is known about the identity of these transient intermediates, the mechanistic factors that enable metal-oxido species to accomplish such difficult reactions are still incomplete. For synthetic metal-oxido species, C-H bond cleavage is often mechanistically described as synchronous, proton-coupled electron transfer (PCET). However, data have emerged that suggest that the basicity of the M-oxido unit is the key determinant in achieving enzymatic function, thus requiring alternative mechanisms whereby proton transfer (PT) has a more dominant role than electron transfer (ET). To bridge this knowledge gap, the reactivity of a monomeric MnIV-oxido complex with a series of external substrates was studied, resulting in a spread of over 104 in their second-order rate constants that tracked with the acidity of the C-H bonds. Mechanisms that included either synchronous PCET or rate-limiting PT, followed by ET, did not explain our results, which led to a proposed PCET mechanism with asynchronous transition states that are dominated by PT. To support this premise, we report a semiempirical free energy analysis that can predict the relative contributions of PT and ET for a given set of substrates. These findings underscore why the basicity of M-oxido units needs to be considered in C-H functionalization.

Theoretical Study of Radical Inactivation, LOX Inhibition, and Iron Chelation: The Role of Ferulic Acid in Skin Protection against UVA Induced Oxidative Stress.

Ferulic acid (FA) is used in skin formulations for protection against the damaging actions of the reactive oxygen species (ROS) produced by UVA radiation. Possible underlying protective mechanisms are not fully elucidated. By considering the kinetics of proton-coupled electron transfer (PCET) and radical-radical coupling (RRC) mechanisms, it appears that direct scavenging could be operative, providing that a high local concentration of FA is present at the place of •OH generation. The resulting FA phenoxyl radical, after the scavenging of a second •OH and keto-enol tautomerization of the intermediate, produces 5-hydroxyferulic acid (5OHFA). Inhibition of the lipoxygenase (LOX) enzyme, one of the enzymes that catalyse free radical production, by FA and 5OHFA were analysed. Results of molecular docking calculations indicate favourable binding interactions of FA and 5OHFA with the LOX active site. The exergonicity of chelation reactions of the catalytic Fe2+ ion with FA and 5OHFA indicate the potency of these chelators to prevent the formation of •OH radicals via Fenton-like reactions. The inhibition of the prooxidant LOX enzyme could be more relevant mechanism of skin protection against UVA induced oxidative stress than iron chelation and assumed direct scavenging of ROS.

Combining Structural with Functional Model Properties in Iron Synthetic Analogue Complexes for the Active Site in Rabbit Lipoxygenase.

Iron complexes that model the structural and functional properties of the active iron site in rabbit lipoxygenase are described. The ligand sphere of the mononuclear pseudo-octahedral cis-(carboxylato)(hydroxo)iron(III) complex, which is completed by a tetraazamacrocyclic ligand, reproduces the first coordination shell of the active site in the enzyme. In addition, two corresponding iron(II) complexes are presented that differ in the coordination of a water molecule. In their structural and electronic properties, both the (hydroxo)iron(III) and the (aqua)iron(II) complex reflect well the only two essential states found in the enzymatic mechanism of peroxidation of polyunsaturated fatty acids. Furthermore, the ferric complex is shown to undergo hydrogen atom abstraction reactions with O-H and C-H bonds of suitable substrates, and the bond dissociation free energy of the coordinated water ligand of the ferrous complex is determined to be 72.4 kcal·mol-1. Theoretical investigations of the reactivity support a concerted proton-coupled electron transfer mechanism in close analogy to the initial step in the enzymatic mechanism. The propensity of the (hydroxo)iron(III) complex to undergo H atom abstraction reactions is the basis for its catalytic function in the aerobic peroxidation of 2,4,6-tri(tert-butyl)phenol and its role as a radical initiator in the reaction of dihydroanthracene with oxygen.

Electrochemical and Mechanistic Study of Oxidative Degradation of Favipiravir by Electrogenerated Superoxide through Proton-Coupled Electron Transfer.

Electrochemical analyses aided by density functional theory calculations were used to investigate the oxidative degradation of pyrazine antiviral drugs, 3-hydroxypyrazine-2-carboxamide (T-1105) and 6-fluoro-3-hydroxypyrazine-2-carboxamide (favipiravir, T-705), by the electrogenerated superoxide radical anion (O2•–). T-1105 and T-705 are antiviral RNA nucleobase analogues that selectively inhibit the RNA-dependent RNA polymerase. They are expected as a drug candidate against various viral infections, including COVID-19. The pyrazine moiety was decomposed by O2•– through proton-coupled electron transfer (PCET). Our results show that its active form, pyrazine-ribofuranosyl-5′-triphosphate, is easily oxidized under inflamed organs by overproduced O2•– through the PCET mechanism in the immune system. This mechanistic study implies that the oxidative degradation of pyrazine derivatives will be prevented by controlling the PCET through simple modification of the pyrazine structure.

SET and HAT/PCET acid-mediated oxidation processes in helical shaped fused bis-phenothiazines.

Helical shaped fused bis‐phenothiazines 1–9 have been prepared and their red‐ox behaviour quantitatively studied. Helicene radical cations (Hel.+) can be obtained either by UV‐irradiation in the presence of PhCl or by chemical oxidation. The latter process is extremely sensitive to the presence of acids in the medium with molecular oxygen becoming a good single electron transfer (SET) oxidant. The reaction of hydroxy substituted helicenes 5–9 with peroxyl radicals (ROO.) occurs with a ‘classical’ HAT process giving HelO. radicals with kinetics depending upon the substitution pattern of the aromatic rings. In the presence of acetic acid, a fast medium‐promoted proton‐coupled electron transfer (PCET) process takes place with formation of HelO. radicals possibly also via a helicene radical cation intermediate. Remarkably, also helicenes 1–4, lacking phenoxyl groups, in the presence of acetic acid react with peroxyl radicals through a medium‐promoted PCET mechanism with formation of the radical cations Hel.+. Along with the synthesis, EPR studies of radicals and radical cations, BDE of Hel‐OH group (BDEOH), and kinetic constants (kinh ) of the reactions with ROO. species of helicenes 1–9 have been measured and calculated to afford a complete rationalization of the redox behaviour of these appealing chiral compounds.

What Triggers the Cleavage of the Co–C5′ Bond in Coenzyme B12-Dependent Itaconyl-CoA Methylmalonyl-CoA Mutase?

Adenosylcobalamin (AdoCbl)-dependent enzymes catalyze complex radical-mediated reactions initiated by homolytic cleavage of the organometallic Co–C5′ bond of the cofactor (AdoCbl) upon substrate binding. Several mechanistic proposals for the activation of the Co–C5′ bond were previously put forward, but none can fully explain the trillion-fold rate enhancement that is observed for cleavage of the Co–C5′ bond in enzymes as compared to AdoCbl in solution. Thus, how the arrival of a substrate triggers the cleavage of the Co–C5′ bond in these enzymes remains an open question. Recently, two crystal structures for AdoCbl-dependent methylmalonyl-CoA mutase (MCM) were reported and provide the opportunity to reinvestigate this long-standing issue. We investigated the activation of the Co–C5′ bond using substrate-free MCM and inhibitor-bound MCM (inhibitor = itaconyl-CoA, I-CoA) by computing the bond dissociation energy (BDE) by utilizing the ONIOM-based quantum mechanics/molecular mechanics (QM/MM) method. The BDE potential energy curves revealed that there is an insensitivity of the Co–C5′ BDE to substrate binding and the energy barrier for cleavage for substrate-free MCM and MCM–[I-CoA] is nearly identical (22.2 vs 22.7 kcal/mol, respectively). This observation puts into question previously reported hypotheses that substrate-induced conformational changes reduce the BDE and trigger the cleavage of the Co–C5′ bond. The present QM/MM results also indicate that the energy barrier for homolytic cleavage of the Co–C5′ bond in both substrate-free MCM and MCM–[I-CoA] is lower than the energy barrier for the isolated cofactor. While the protein environment clearly reduces the barrier for the Co–C5′ bond cleavage, the reduction to the energy barrier is too small to fully explain the trillion-fold rate acceleration. Hence, we also explored the role of Tyr105 as a redox center and the feasibility of a proton-coupled electron transfer (PCET) mechanism. It was found that the [AdoCbl]•–/TyrO• diradical state is the lowest electronic state, implying that the Tyr105 residue can play a crucial role in triggering the cleavage of the Co–C5′ bond in MCM–[I-CoA] by facilitating an ET to the AdoCbl cofactor via a PCET mechanism.

Models to study photoinduced multiple proton coupled electron transfer processes

In water-oxidizing photosynthetic organisms, excitation of the reaction-center chlorophylls (P680) triggers a cascade of electron and proton transfer reactions that establish charge separation across the membrane and proton-motive force. An early oxidation step in this process involves proton-coupled electron transfer (PCET) via a tyrosine-histidine redox relay (Yz-H190). Herein, we report the synthesis and structural characterization of two isomeric dyads designed to model this PCET process. Both are based on the same high potential fluorinated porphyrin (model for P680), linked to isomeric pyridylbenzimidazole-phenols (models for Yz-H190). The two isomeric dyads have different hydrogen bond frameworks, which is expected to change the PCET photooxidation mechanism. In these dyads, 1H NMR evidence indicates that in one dyad the hydrogen bond network would support a Grotthuss-type proton transfer process, whereas in the other the hydrogen bond network is interrupted. Photoinduced one-electron, two-proton transfer is expected to occur in the fully hydrogen-bonded dyad upon oxidation of the phenol by the excited state of the porphyrin. In contrast for the isomer with the interrupted hydrogen bond network, an ultrafast photoinduced one-electron one-proton transfer process is anticipated, followed by a much slower proton transfer to the terminal proton acceptor. Understanding the nature of photoinduced PCET mechanisms in these biomimetic models will provide insights into the design of future generations of artificial constructs involved in energy conversion schemes.

A Quinol Anion as Catalytic Intermediate Coupling Proton Translocation With Electron Transfer in E. coli Respiratory Complex I.

Energy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, plays a major role in cellular energy metabolism. It couples NADH oxidation and quinone reduction with the translocation of protons across the membrane, thus contributing to the protonmotive force. Complex I has an overall L-shaped structure with a peripheral arm catalyzing electron transfer and a membrane arm engaged in proton translocation. Although both reactions are arranged spatially separated, they are tightly coupled by a mechanism that is not fully understood. Using redox-difference UV-vis spectroscopy, an unknown redox component was identified in Escherichia coli complex I as reported earlier. A comparison of its spectrum with those obtained for different quinone species indicates features of a quinol anion. The re-oxidation kinetics of the quinol anion intermediate is significantly slower in the D213GH variant that was previously shown to operate with disturbed quinone chemistry. Addition of the quinone-site inhibitor piericidin A led to strongly decreased absorption peaks in the difference spectrum. A hypothesis for a mechanism of proton-coupled electron transfer with the quinol anion as catalytically important intermediate in complex I is discussed.

The Interaction of Porcine Dihydropyrimidine Dehydrogenase with the Chemotherapy Sensitizer: 5-Ethynyluracil.

Dihydropyrimidine dehydrogenase (DPD) is a complex enzyme that reduces the 5,6-vinylic bond of pyrimidines, uracil, and thymine. 5-Fluorouracil (5FU) is also a substrate for DPD and a common chemotherapeutic agent used to treat numerous cancers. The reduction of 5FU to 5-fluoro-5,6-dihydrouracil negates its toxicity and efficacy. Patients with high DPD activity levels typically have poor outcomes when treated with 5FU. DPD is thus a central mitigating factor in the treatment of a variety of cancers. 5-Ethynyluracil (5EU) covalently inactivates DPD by cross-linking with the active-site general acid cysteine in the pyrimidine binding site. This reaction is dependent on the simultaneous binding of 5EU and nicotinamide adenine dinucleotide phosphate (NADPH). This ternary complex induces DPD to become activated by taking up two electrons from the NADPH. The covalent inactivation of DPD by 5EU occurs concomitantly with this reductive activation with a rate constant of ∼0.2 s-1. This kinact value is correlated with the rate of reduction of one of the two flavin cofactors and the localization of a mobile loop in the pyrimidine active site that places the cysteine that serves as the general acid in catalysis proximal to the 5EU ethynyl group. Efficient cross-linking is reliant on enzyme activation, but this process appears to also have a conformational aspect in that nonreductive NADPH analogues can also induce a partial inactivation. Cross-linking then renders DPD inactive by severing the proton-coupled electron transfer mechanism that transmits electrons 56 Å across the protein.

Electrochemical and Mechanistic Study of Superoxide Elimination by Mesalazine through Proton-Coupled Electron Transfer.

The elimination of superoxide radical anions (O2•−) by 5-amino-2-hydroxybenzoic acid (mesalazine, 5-ASA), 4-amino-2-hydroxybenzoic acid (4-ASA), and related compounds used for ulcerative colitis treatment was investigated using cyclic voltammetry and electron spin resonance (ESR) analyses aided by density functional theory (DFT) calculations. Quasi-reversible O2/O2•− redox was found to be modified by the compounds, suggesting that an acid–base reaction in which a hydroperoxyl radical (HO2•) is formed from O2•− occurs. However, the deprotonated 5-ASA anion can eliminate O2•− through proton-coupled electron transfer (PCET), forming a radical product. This electron transfer (ET) was confirmed by ESR analysis. The 4-aminophenol moiety in 5-ASA plays an important role in the PCET, involving two proton transfers and one ET based on π-conjugation. The electrochemical and DFT results indicated that O2•− elimination by 5-ASA proceeds efficiently through the PCET mechanism after deprotonation of the 1-carboxyl group. Thus, 5-ASA may act as an anti-inflammatory agent in the alkali intestine through PCET-based O2•− elimination.

Understanding the Mechanism of Proton-Coupled Electron Transfer in the Bioinspired Artificial Photosynthetic Mimic, Benzimidazole Phenol Porphyrin

Understanding the Mechanism of Proton-Coupled Electron Transfer in the Bioinspired Artificial Photosynthetic Mimic, Benzimidazole Phenol Porphyrin

Theoretical Description of the Primary Proton-Coupled Electron Transfer Reaction in the Cytochrome bc1 Complex.

The cytochrome bc1 complex is a transmembrane enzymatic protein complex that plays a central role in cellular energy production and is present in both photosynthetic and respiratory chain organelles. Its reaction mechanism is initiated by the binding of a quinol molecule to an active site, followed by a series of charge transfer reactions between the quinol and protein subunits. Previous work hypothesized that the primary reaction was a concerted proton-coupled electron transfer (PCET) reaction because of the apparent absence of intermediate states associated with single proton or electron transfer reactions. In the present study, the kinetics of the primary bc1 complex PCET reaction is investigated with a vibronically nonadiabatic PCET theory in conjunction with all-atom molecular dynamics simulations and electronic structure calculations. The computed rate constants and relatively high kinetic isotope effects are consistent with experimental measurements on related biomimetic systems. The analysis implicates a concerted PCET mechanism with significant hydrogen tunneling and nonadiabatic effects in the bc1 complex. Moreover, the employed theoretical framework is shown to serve as a general strategy for describing PCET reactions in bioenergetic systems.

High-valence-state Ni–Fe bimetallic phosphonate nanoribbons catalyst for enhanced photocatalytic and electrocatalytic oxygen production

The design and synthesis of economy and efficiency materials for oxygen evolution reaction (OER) have been a continuous hot spot in the field of scientific study. Herein, a high-valence-state two-dimension (2D) NiFe phosphonate-based (NiFeP) nanoribbons catalyst has been constructed through a one-step solvothermal process. The NiFeP nanoribbons exhibit highly active in both photocatalytic and electrocatalytic water oxidation due to the 2D nanoribbons and high-valence Ni3+ sites. The 2D nanoribbons not only provide more reactive sites for OER but also shorten bulk diffusion distance with better photoexcited carrier transport from the interior to the surface. Meanwhile, the existence of high-valence Ni3+ could be acted as an efficient redox site to reduce the overpotential and facilitate the catalytic reaction. In consequence, the NiFeP nanoribbons catalyst demonstrates a superior O2 yield of 65.7% and O2 production rate of 25.97 umol s−1 g−1, which are comparable or even much higher than those other reported transition metal oxide photocatalysts. At last, the possible proton-coupled electron transfer mechanism is also proposed. This study not only demonstrates the potential of a low-cost metal phosphonate OER catalyst but also provides a referential system for the fabrication of high activity and stability catalysts toward replacing noble metals for energy storage and conversion. High-valence-state 2D NiFe phosphonate-based nanoribbons catalyst has been constructed for the first time through a one-step solvothermal process without any organic additives or template agent. The as-prepared catalyst of NiFeP nanoribbons exhibits highly active in both photocatalytic and electrocatalytic water oxidation.