Redox Interactions Research Articles

Redox-capacitor to connect electrochemistry to redox-biology

It is well-established that redox-reactions are integral to biology for energy harvesting (oxidative phosphorylation), immune defense (oxidative burst) and drug metabolism (phase I reactions), yet there is emerging evidence that redox may play broader roles in biology (e.g., redox signaling). A critical challenge is the need for tools that can probe biologically-relevant redox interactions simply, rapidly and without the need for a comprehensive suite of analytical methods. We propose that electrochemistry may provide such a tool. In this tutorial review, we describe recent studies with a redox-capacitor film that can serve as a bio-electrode interface that can accept, store and donate electrons from mediators commonly used in electrochemistry and also in biology. Specifically, we (i) describe the fabrication of this redox-capacitor from catechols and the polysaccharide chitosan, (ii) discuss the mechanistic basis for electron exchange, (iii) illustrate the properties of this redox-capacitor and its capabilities for promoting redox-communication between biology and electrodes, and (iv) suggest the potential for enlisting signal processing strategies to "extract" redox information. We believe these initial studies indicate broad possibilities for enlisting electrochemistry and signal processing to acquire "systems level" redox information from biology.

Redox interactions between structurally different alkylresorcinols and iron(III) in aqueous media: frozen-solution 57Fe Mössbauer spectroscopic studies, redox kinetics and quantum chemical evaluation of the alkylresorcinol reactivities

Iron(III)-containing aqueous solutions of 5-methylresorcinol (5-MR), 5-n-propylresorcinol (5-n-PR) and 4-n-hexylresorcinol (4-n-HR) at pH ~ 3 were studied by means of 57Fe transmission Mossbauer spectroscopy. Kinetic considerations were applied to the redox reactions. Density Functional Theory (DFT) calculations were performed for the alkylresorcinol (AR) molecules and their non-alkylated analogue (resorcinol). Mossbauer spectra consisted of quadrupole doublets assigned to high-spin Fe(III) and Fe(II) species. From changes in their relative spectral areas, a gradual reduction of Fe(III) by all the ARs studied was observed. However, significant differences were found for the reduction rates among the ARs. The following series of the reduction rates was established by means of Mossbauer spectroscopy: 4-n-HR ≫ 5-MR > 5-n-PR, supplemented by rate constants calculated using a kinetic model. DFT calculations resulted in the following series: 4-n-HR ≫ 5-n-PR > 5-MR ≫ resorcinol (the latter is not oxidised under the conditions applied). The reversed order of the experimentally observed 5-MR and 5-n-PR oxidation rates may be explained in terms of their different kinetic parameters related to their structure.

Atomistic structure of a spinel Li4Ti5O12(111) surface elucidated by scanning tunneling microscopy and medium energy ion scattering spectrometry

Spinel lithium titanate (Li4Ti5O12, LTO) is one of the promising anode materials for high-performance lithium-ion batteries (LIBs). It is crucial to investigate atomistic structures of LTO surfaces to understand the phenomena at LTO/electrolyte interfaces such as CO2-gas generation which greatly affects the performance and safety of LIBs. By applying scanning tunneling microscopy (STM) and medium energy ion scattering spectrometry (MEIS) to a LTO(111) film prepared from a TiO2 wafer, we found that there exist two kinds of Li-terminated (111) terraces bounded by steps with different heights. In the major terraces, the top hexagonal Li layer is stacked above the oxygen layer, while the top Li layer is stacked above the Ti–Li layer in the minor terraces. The relative stability between the two surface structures seems to depend on the atmosphere due to different stoichiometry. For the major terraces, the LTO surface should have electronic holes due to oxygen-rich stoichiometry, which is a possible origin of CO2 generation via redox interaction with electrolyte molecules.

Copper Redox Transformation and Complexation by Reduced and Oxidized Soil Humic Acid. 1. X-ray Absorption Spectroscopy Study

Natural organic matter (NOM) exerts strong influence on copper speciation and bioavailability in soils and aquatic systems. In redox-dynamic environments, electron transfer reactions between copper and redox-active moieties of NOM may trigger Cu(I) and Cu(0) formation. To date, little is known about Cu-NOM redox interactions and Cu(I) binding to NOM. Here, we present X-ray absorption spectroscopy results on copper redox transformations upon addition of Cu(II) or Cu(I) to untreated and electrochemically reduced soil humic acid (HA) under oxic and anoxic conditions. Both untreated and reduced HA mediated copper redox transformations. Under anoxic conditions, Cu(II) and Cu(I) added to reduced HA were primarily complexed and thereby stabilized as Cu(I)-HA at low loadings, whereas high copper loadings resulted in the additional formation of Cu(0) nanoparticles (16-64% of total copper). Cu(I) bound to HA was predominantly 2-fold coordinated and to a lower extent 3- to 4-fold coordinated, with a contribution of at least one nitrogen and/or sulfur ligand group. Under oxic conditions, Cu(II)-HA complexes prevailed, but smaller fractions of copper were also stabilized as Cu(I)-HA in a 3- to 4-fold coordination. Our results show that Cu-HA redox interactions are strongly affected by binding of Cu(II) and Cu(I) to HA and that HA contributes to the stabilization of Cu(I) against disproportionation.

Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases.

Ero1-α and endoplasmic reticulum (ER) oxidoreductases of the protein disulfide isomerase (PDI) family promote the efficient introduction of disulfide bonds into nascent polypeptides in the ER. However, the hierarchy of electron transfer among these oxidoreductases is poorly understood. In this paper, Ero1-α-associated oxidoreductases were identified by proteomic analysis and further confirmed by surface plasmon resonance. Ero1-α and PDI were found to constitute a regulatory hub, whereby PDI induced conformational flexibility in an Ero1-α shuttle cysteine (Cys99) facilitated intramolecular electron transfer to the active site. In isolation, Ero1-α also oxidized ERp46, ERp57, and P5; however, kinetic measurements and redox equilibrium analysis revealed that PDI preferentially oxidized other oxidoreductases. PDI accepted electrons from the other oxidoreductases via its a' domain, bypassing the a domain, which serves as the electron acceptor from reduced glutathione. These observations provide an integrated picture of the hierarchy of cooperative redox interactions among ER oxidoreductases in mammalian cells.

Spectroscopic and Electrochemical Characterization of the [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Reversible Redox Behavior and Interactions between Electron Transfer Centers

Characterizing a new hydrogenase: The newly isolated [NiFeSe] hydrogenase from Desulfovibrio vulgaris Miyazaki F displays catalytic properties distinct from other hydrogenase proteins. Here we apply site-specific spectroscopic and electrochemical techniques to characterize these unique features at the molecular level.

Redox interactions between Fe and cysteine: Spectroscopic studies and multiplet calculations

The biogeochemical cycle of Fe is intricately linked with that of organic matter. Cysteine represents an organic molecule with functionalities (O, S, N functional groups) and a C backbone that may mimic the functional groups present in organic matter from terrestrial and aquatic environments. In the present study we explore the redox speciation and coordination environment of Fe and the roles of the various ligand atoms of cysteine (C, N, S) in iron-organic redox coupling and transformations. The changes in oxidation state of Fe, C, N, and S in laboratory-synthesized Fe(II)–cysteine (synthesized from ferrous sulfate) and Fe(III)–cysteine (synthesized from ferric nitrate) complexes are monitored as a function of time using synchrotron X-ray absorption spectroscopy (Fe L2,3-edge XANES; C, N and S K-edge XANES; Fe K-edge EXAFS) and theoretical multiplet calculations using the program CTM4XAS (Charge Transfer Multiplet for X-ray Absorption Spectroscopy). CTM4XAS calculations show that 80% of the total Fe in both the Fe(II)–cysteine and the Fe(III)–cysteine complexes is present as Fe2+ initially (t=0), thus indicating preservation of Fe(II) in Fe(II)–cysteine and reduction of Fe(III) in Fe(III)–cysteine at initial conditions, the latter caused by an internal electron transfer reaction from S of –SH on the cysteine molecule. After 12months, however, ∼60% of the total Fe is present as Fe3+ in the Fe(II)–cysteine complex whereas ∼67% of the total Fe is present as Fe2+ in the Fe(III)–cysteine complex. The fact that a larger proportion of the Fe in the Fe(III)–cysteine complex remained reduced after 12months than that in the Fe(II)–cysteine complex suggests that the reduced Fe in Fe(III)–cysteine after 12months is further stabilized via preferential binding with the donor atoms of cysteine. Stabilization via preferential binding is supported by a coordination environment that changed from tetrahedral Fe2+ binding to S at a distance of 2.3Å at t=0 for both Fe(II,III)–cysteine complexes, to Fe3+ in an octahedral coordination with O/N atoms at a distance of 2.05Å (most prevalent in Fe(II)–cysteine) and Fe2+ in tetrahedral coordination with S/O/N atoms at an average distance of 2.15Å (most prevalent in Fe(III)–cysteine) at t=12months. Redox changes in the –NH2 and –SH groups of cysteine accompanied the Fe redox changes thus reflecting the true potential of cysteine as a redox ligand. Our studies of the Fe(II,III)–cysteine complexes add valuable information to the existing literature on the redox chemistry of Fe–cysteine systems by shedding light on the electron exchange pathways that may occur within the complexes and by providing a detailed depiction of the iron-ligand structure and coordination. The presence and persistence of Fe(II) or Fe(III) in complexes with soluble organics have implications for Fe biological availability and Fe mobility and transport in terrestrial as well as in aquatic environments.

Enzymatic Writing to Soft Films: Potential to Filter, Store, and Analyze Biologically Relevant Chemical Information

Sensor‐based chemical analyses commonly enlist either the molecular recognition capabilities of biology (e.g., enzyme biosensors) or advanced information processing algorithms (e.g., the electronic nose). Here, a hybrid approach is proposed in which an enzyme is used to “filter” chemical information and write this information to a film which then serves as a permanent storage medium that can be ‘read’ repeatedly, interactively, and by multiple sensor modalities. This approach is demonstrated by analyzing common dietary phenols that are reported to offer health benefits. Specifically, the enzyme tyrosinase is used to convert these phenols into reactive quinones that graft (i.e., write) to a chitosan film. Grafting can be detected by optical, mechanical, and electrochemical sensors. Importantly, grafting confers redox activity to the films and this redox activity can be probed interactively by advanced electrochemical methods that allow the intrinsic redox reactivities to be compared, redox interactions to be identified, and biologically relevant redox activities to be examined. The transfer of chemical and biological information to a film is envisioned to provide broader access to the extensive capabilities offered by sensor technologies and signal processing methodologies.

Mössbauer study of the effect of pH on the rate of redox interactions between iron(III) and 4-n-hexylresorcinol in aqueous media

Mossbauer spectroscopy is used for a comparative study of the rate of iron(III) reduction by 4-n-hexylresorcinol (4-n-HR, a chemical analog of microbial autoregulators excreted by cells into the environment that allow intercellular communication) in aqueous media in the pH range of 1.5–4.5 simulating acidic soil conditions. The concomitant process of 4-n-HR oxidation is monitored using UV spectrophotometry.

A review of microbial redox interactions with structural Fe in clay minerals

AbstractVirtually all 2:1 clay minerals contain some Fe in their crystal structure, which may undergo redox reaction with surrounding redox-active species causing potentially significant changes in the chemical and physical properties of the clay mineral and its surrounding matrix. This phenomenon was originally of interest mostly as a laboratory experiment using strong inorganic reduction agents, but the discovery that the structural Fe could be reduced by microorganisms in natural soils and sediments opened the way for this to become a practical method for altering the chemical and physical properties of soils and sedimentsin situ. The purpose of this report was to review the body of literature that has been published since the inception of this field of inquiry and to complement, update, and complete three other reviews that have been published during the intervening years. Studies of microbial reduction of structural Fe in smectites have revealed the extent of reduction, effects on chemical and physical properties, reversibility (or lack thereof) of microbial reduction, stoichiometry, possible reaction mechanism, and types of organisms involved. Some organisms are also capable of oxidizing structural Fe, such as in biotite or reduced smectite, while one appears to be able to do both. Illitic layers resist reduction by microorganisms, but this can be partially overcome by the presence of an electron shuttle compound such as anthraquinone-2,6-disulfonate, which also enhances the extent of reduction in smectites. Microorganisms may be employed as an in situ reducing agent to drive redox cycles for structural Fe in constituent clay minerals of soils and sediments, which in turn can serve as an abiotic source for redox-mediated remediation of environmental contaminants.

On the Reactivity of Carbon Supported Pd Nanoparticles during NO Reduction: Unraveling a Metal–Support Redox Interaction

Pd nanoparticles (NPs) were successfully obtained by the reduction of PdCl2 with L-ascorbic acid, whose morphology was revealed by HRTEM to be a worm-like system, formed by linked crystallite clusters with an average short-axis diameter of 5.42 nm. In situ UV-vis absorption measurements were used to monitor their formation, while XPS and XRD characterization confirmed the NPs' metallic state. A straightforward way to support the obtained Pd NPs on activated carbon (AC) was used to prepare a catalyst for NO decomposition reaction. The Pd/AC catalysts proved to be highly active in the temperature range of 323 to 673 K, and a redox mechanism is proposed, where the catalyst's active sites are oxidized by NO and reduced by carbon, emitting CO2 and enhancing their capacity to absorb and dissociate NO.

Protein disulfide-isomerase interacts with soluble guanylyl cyclase via a redox-based mechanism and modulates its activity.

NO binds to the receptor sGC (soluble guanylyl cyclase), stimulating cGMP production. The NO-sGC-cGMP pathway is a key component in the cardiovascular system. Discrepancies in sGC activation and deactivation in vitro compared with in vivo have led to a search for endogenous factors that regulate sGC or assist in cellular localization. In our previous work, which identified Hsp (heat-shock protein) 70 as a modulator of sGC, we determined that PDI (protein disulfide-isomerase) bound to an sGC-affinity matrix. In the present study, we establish and characterize this interaction. Incubation of purified PDI with semi-purified sGC, both reduced and oxidized, resulted in different migration patterns on non-reducing Western blots indicating a redox component to the interaction. In sGC-infected COS-7 cells, transfected FLAG-tagged PDI and PDI CXXS (redox active site 'trap mutant') pulled down sGC. This PDI-sGC complex was resolved by reductant, confirming a redox interaction. PDI inhibited NO-stimulated sGC activity in COS-7 lysates, however, a PDI redox-inactive mutant PDI SXXS did not. Together, these data unveil a novel mechanism of sGC redox modulation via thiol-disulfide exchange. Finally, in SMCs (smooth muscle cells), endogenous PDI and sGC co-localize by in situ proximity ligation assay, which suggests biological relevance. PDI-dependent redox regulation of sGC NO sensitivity may provide a secondary control over vascular homoeostasis.

Interaction of hydrogen with Cu–Zn mixed oxide model methanol synthesis catalyst

Interaction of hydrogen with model Cu–Zn methanol synthesis catalyst prepared by decomposition of mixed hydroxicarbonate is studied by inelastic neutron scattering, in situ FTIR/MS, and thermal analysis. Reduced (Cu0.08,Zn0.92)O mixed oxide accumulates 6H/Cu, mainly as hydride, hydroxyl and formate species. The reduction of copper in the (Cu,Zn)O mixed oxide occurs via a reversible redox interaction with H2 and absorption of protons as OH−-groups with ν=3250cm−1 and δ≈1430–1480cm−1. Kinetic and thermodynamic parameters of this process are evaluated. The weight loss during the reduction is due to the decomposition of the residual carbonate groups to CO2 via formate intermediates, which occurs in the presence of hydrogen. Exposure of (Cu,Zn)O to air prior to the reduction strongly affects the kinetic parameters of the reduction process.

Interaction of Cr(III) and Cr(VI) with Hematite Studied by Second Harmonic Generation

The fate of chromium in the environment relies heavily on its redox chemistry and interaction with iron oxide surfaces. Atomic layer deposition was used to deposit a 10 nm film of polycrystalline α-Fe2O3 (hematite) onto a fused silica substrate which was analyzed using second harmonic generation (SHG), a coherent, surface-specific, nonlinear optical technique. Specifically, the χ(3) technique was used to investigate the adsorption of Cr(III) and Cr(VI) to the hematite/water interface under flow conditions at pH 4 with 10 mM NaCl. We observed partially irreversible adsorption of Cr(III), the extent of which was found to be dependent on the concentration of Cr(III) ions in solution. This result was confirmed using X-ray photoelectron spectroscopy. The interaction of Cr(III) with hematite is compared with the adsorption of Cr(III) to the silica/water interface, which is the substrate for the ALD-prepared hematite films, and found to be fully reversible under the same experimental conditions. The observed binding constant for Cr(III) interacting with the silica surface was found to be 4.0(6) × 103 M–1, which corresponds to an adsorption free energy of −30.5(4) kJ/mol when referenced to 55.5 M water. The surface charge density at maximum metal ion surface coverage was found to be 0.005(1) C/m2, which corresponds to 1.0 × 1012 ions/cm2 assuming a +3 charge for chromium. In contrast, the observed binding constant for Cr(III) interacting reversibly with the hematite surface was calculated to be 2(2) × 104 M–1, corresponding to an adsorption free energy of −35(2) kJ/mol when referenced to 55.5 M water. The surface charge density at maximum metal ion surface coverage was found to be 0.004(5) C/m2 for the reversibly bound chromium species, which corresponds to 8.3 × 1011 reversibly bound ions per cm2, again assuming a +3 charge of chromium. The data also allows us to estimate that about 6.7 × 1012 Cr(III) ions are irreversibly bound per cm2 hematite at saturation coverage. The results of this investigation suggest that the use of hematite in permeable reactive barriers, for cost-effective chromium remediation, allows for Cr(III) remediation at very low concentrations through adsorptive and redox processes but quickly renders the barriers ineffective at high chromium concentrations due to surface saturation.

Reverse Engineering To Suggest Biologically Relevant Redox Activities of Phenolic Materials

Phenolics are among the most abundant redox-active organics in nature, but the intractability of phenolic materials (e.g., melanin) has precluded study of their biological activities and functions. Previous studies demonstrated that a model abiotic catecholic matrix can rapidly exchange electrons with biological oxidants and reductants without the need for enzymes. Here, a novel electrochemically based reverse engineering approach was employed to probe redox interactions between this model matrix and a population of bacteria. Specifically, this method employs redox-active natural products (e.g., pyocyanin) to shuttle electrons between the bacteria and the abiotic matrix, and imposed oscillating potential inputs to engage redox-cycling mechanisms that switch the matrix's redox state. The oscillating output currents were observed to be amplified, gated, and partially rectified, while the overall magnitude and direction of electron flow across the matrix depended on the biological and environmental context. These response characteristics support hypotheses that natural phenolic materials may be integral to extracellular electron transport for processes that include anaerobic respiration, redox signaling, and redox-effector action.

Nanosized zinc and magnesium ferrites obtained from PVA–metal nitrates’ solutions

The paper presents a study regarding the possibility of obtaining zinc and magnesium ferrites starting from poly(vinyl alcohol)–metal nitrates solutions. By controlled heating of these solutions, a redox interaction takes place leading to the formation of some coordination compounds of the involved metal cations with the oxidation products of poly(vinyl alcohol) (PVA). FT-IR spectroscopy has evidenced the disappearance of the NO3− anions at 140 °C due to the redox interaction with PVA. Thermal analysis evidenced the difference in the interaction of the individual metal nitrates and PVA and thus the particularity of the preparation of each ferrite. The thermal decomposition of the synthesized precursors was finished below 400 °C as resulting from both thermal analysis and FT-IR spectroscopy. The obtained ferrites powders consist of fine nanoparticle with diameters ranging from 10 to 30 nm for the powders annealed at 500 °C, as resulting from the SEM images. The specific surface area of the powders obtained at 500 °C was 32.2 m2 g−1 for ZnFe2O4 and 21.7 m2 g−1 for MgFe2O4, characteristic of nanoscaled powders. The increasing of the annealing temperature at 1,000 °C leads to sintering of both ferrites, more advanced in the case of zinc ferrite.

Low-temperature generation of strong basicity via an unprecedented guest–host redox interaction

An unprecedented guest-host redox strategy is developed to generate strong basicity on mesoporous silica, which breaks the tradition of thermally induced decomposition of precursors. New materials possessing ordered mesostructure, strong basicity, and excellent catalytic activity are thus successfully fabricated at a low temperature.

Elemental chemistry of sand-boil discharge used to trace variable pathways of seepage beneath levees during the 2011 Mississippi River flood

Shortly after peak stage of the 2011 Mississippi River flood, water samples were collected from the river, from sand boils near the toe of the levee, and from actively flowing relief wells over a 55 km stretch north of Vicksburg, MS. Two distinct pathways for seepage under the levee were identified based on the elemental composition of water samples. Sand boil discharge was similar to water from relief wells only at a location where the levee sits on ancient channel fill deposits. Seepage at this site is forced along a deeper pathway beneath the fine-grained channel fill. Where the levee sits on sandy point bar deposits, shallow flow beneath the levee is unimpeded. The chemical composition of discharge from sand boils at these sites was clearly not just river water, nor a simple mixture of river and groundwater, but appears to reflect unique weathering or redox interactions occurring within the upper portion of the alluvial aquifer. Distinguishing shallow and deep seepage pathways may prove useful for evaluating site specific risk of levee failure.

Effect of gamma irradiation on chromate sorption over magnetite surface

Aqueous chromate sorption on suspended magnetite in the presence of gamma irradiation has been evaluated. Kinetics of chromate removal was evaluated using Lagergren's absorption model. Chromate removal with respect to the accumulated dose followed a Lagergren's pseudo-first-order kinetic model. A comparison of kinetics of chromate removal with respect to total accumulated dose for gamma irradiation experiment vis-à-vis with respect to time of treatment for different isothermal interactions has been undertaken. Rate constants indicate that the chromate removed per minute in isothermal equilibration at 80 °C is comparable to the chromate removed per kilogrey of gamma irradiation received. There is a redox interaction between the chromate and the ferrous of the suspended magnetite which was confirmed by X ray photo electron spectroscopy (XPS) analysis. This process reaches a saturation much before the consumption of entire ferrous ions of magnetite, indicating a passivating nature of the product. The effect of radiation on both chromate solution and dispersed magnetite to alter the redox process could be ascertained. Gaussian–Lorenzian peak fittings to the XPS data have been carried out to evaluate the chemical composition of the deposited chromium and the resultant change in the chemical composition of the iron in the oxide lattice. This indicated that the magnetite equilibrated with chromate under gamma irradiation resulted in a different surface composition as compared with the one obtained in absence of gamma irradiation. XPS data indicated the presence of hydroxyl group and oxide group attached to both iron and chromium moieties in case of irradiation, whereas only oxide group was seen with only temperature treatment.

Cytochrome c oxidase heme and Cu centres: Redox and spectral interactions

Cytochrome c oxidase heme and Cu centres: Redox and spectral interactions