RESUMEN
Reverse electrodialysis (RED) power generation using seawater (SW) and river water is expected to be a promising environmentally friendly power generation system. Experiments with large RED stacks are needed for the practical application of RED power generation, but only a few experimental results exist because of the need for large facilities and a large area of ion-exchange membranes (IEMs). In this study, to predict the power output of a large RED stack, the power generation performances of a lab-scale RED stack (40 membrane pairs and 7040 cm2 total effective membrane area) with several IEMs were evaluated. The results were converted to the power output of a pilot-scale RED stack (299 membrane pairs and 179.4 m2 total effective membrane area) via the reference IEMs. The use of low-area-resistance IEMs resulted in lower internal resistance and higher power density. The power density was 2.3 times higher than that of the reference IEMs when natural SW was used. The net power output was expected to be approximately 230 W with a pilot-scale RED stack using low-area-resistance IEMs and natural SW. This value is one of the indicators of the output of a large RED stack and is a target to be exceeded with further improvements in the RED system.
RESUMEN
Patients with chronic granulomatous disease (CGD) who have mutated phagocyte NADPH oxidase are susceptible to infections due to reduced reactive oxygen species production and exhibit autoimmune and inflammatory diseases in the absence of evident infection. Neutrophils and macrophages have been extensively studied since phagocyte NADPH oxidase is mainly found only in them, while the impact of its deficiency on lymphocyte cellularity is less well characterized. We showed herein a zymosan-induced systemic inflammation model that CGD mice deficient in the phagocyte NADPH oxidase gp91phox subunit (NOX2) exhibited more severe thymic atrophy associated with peripheral blood and splenic lymphopenia and reduced lymphopoiesis in the bone marrow in comparison with the wild-type mice. Conversely, the zymosan-exposed CGD mice suffered from more remarkable neutrophilic lung inflammation, circulating and splenic neutrophilia, and enhanced granulopoiesis compared with those in zymosan-exposed wild-type mice. Overall, this study provided evidence that NOX2 deficiency exhibits severe thymic atrophy and lymphopenia concomitant with enhanced neutrophilic inflammation in a zymosan-induced systemic inflammation model.
Asunto(s)
Linfopenia/metabolismo , Linfopoyesis/fisiología , NADPH Oxidasa 2/deficiencia , Síndrome de Respuesta Inflamatoria Sistémica/metabolismo , Timo/metabolismo , Zimosan/toxicidad , Animales , Atrofia , Modelos Animales de Enfermedad , Relación Dosis-Respuesta a Droga , Enfermedad Granulomatosa Crónica/inducido químicamente , Enfermedad Granulomatosa Crónica/metabolismo , Enfermedad Granulomatosa Crónica/patología , Linfopenia/patología , Ratones , Ratones Endogámicos C57BL , Ratones Noqueados , Síndrome de Respuesta Inflamatoria Sistémica/inducido químicamente , Síndrome de Respuesta Inflamatoria Sistémica/patología , Timo/efectos de los fármacos , Timo/patologíaRESUMEN
The present study examined whether luminance values of an edge between regions affect figure-ground perception. A dark-gray or light-gray region was presented on the left (or upper) or right (or lower) side of an edge. Observers reported which region was perceived as a figure. The results in the 0.2° edge width condition showed that dark-gray regions with low luminance edges were perceived as a figure significantly more often than dark-gray regions with high luminance edges. The edge luminance effect occurred, partly occurred, and did not occur when the edge widths were 0.2, 0.5, and 0.8° of visual angle, respectively. These results showed that luminance values of the edge between the regions affected figure-ground perception, and that regions with luminance values closer to that of the edge between the regions were perceived as a figure more often, but only when the edge width was narrow. The edge luminance effect occurred less often as the edge width was increased and would be attributed to similarity grouping between edge and region.
Asunto(s)
Sensibilidad de Contraste/fisiología , Percepción de Forma/fisiología , Reconocimiento Visual de Modelos/fisiología , Femenino , Humanos , MasculinoRESUMEN
Shewanella can transfer electrons to various extracellular electron acceptors. We electrochemically investigated the pathway of extracellular electron transfer from Shewanella strain Hac319 to electrodes. A resting cell suspension of Shewanella strain Hac319 containing lactate produced a steady-state sigmoidal wave in the presence of flavin mononucleotide (FMN) in cyclic voltammetry, but not in the absence of FMN. A harvested cell suspension without cell-washing also produced a similar catalytic wave without any external addition of free FMN. The midpoint potentials of the two sigmoidal waves were identical to the redox potential of free FMN. The data indicate that FMN secreted from the Shewanella strain Hac319 works as an electron-transfer mediator from the cell to electrodes. An addition of cyanide to a resting cell suspension of Shewanella strain Hac319 increased the rate of the FMN reduction in the presence of lactate, while it decreased the respiration rate. By considering the fact that cyanide is coordinated to the heme moiety of hemoproteins and shifts the redox potential to the negative potential side, the data indicate that the electron derived from lactate is predominantly transferred in a down-hill mode from an electron donor with a redox potential more negative than that of FMN without going through outer membrane cytochromes c molecules.
Asunto(s)
Electroquímica/instrumentación , Espacio Extracelular/metabolismo , Shewanella/citología , Shewanella/metabolismo , Cianuros/farmacología , Electrodos , Transporte de Electrón/efectos de los fármacos , Espacio Extracelular/efectos de los fármacos , Mononucleótido de Flavina/metabolismo , Ácido Láctico/metabolismo , Shewanella/efectos de los fármacosRESUMEN
Standard [NiFe]-hydrogenase from Desulfovibrio vulgaris Miyazaki F (DvMF-H2ase) catalyzes the uptake and production of hydrogen (H2) and is a promising biocatalyst for future energy devices. However, DvMF-H2ase experiences oxidative inactivation under oxidative stress to generate Ni-A and Ni-B states. It takes a long time to reactivate the Ni-A state by chemical reduction, whereas the Ni-B state is quickly reactivated under reducing conditions. Oxidative inhibition limits the application of DvMF-H2ase in practical devices. In this research, we constructed a mediated-electron-transfer system by co-immobilizing DvMF-H2ase and a viologen redox polymer (VP) on electrodes. The system can avoid oxidative inactivation into the Ni-B state at high electrode potentials and rapidly reactivate the Ni-A state by electrochemical reduction of VP. H2 oxidation and H+ reduction were realized by adjusting the pH from a thermodynamic viewpoint. Using carbon felt as a working-electrode material, high current densities-up to (200⯱â¯70) and -(100⯱â¯9) mAâ¯cm-3 for the H2-oxidation and H+-reduction reactions, respectively-were attained.
Asunto(s)
Desulfovibrio vulgaris/enzimología , Enzimas Inmovilizadas/metabolismo , Hidrógeno/metabolismo , Hidrogenasas/metabolismo , Biocatálisis , Técnicas Biosensibles , Desulfovibrio vulgaris/química , Desulfovibrio vulgaris/metabolismo , Transporte de Electrón , Activación Enzimática , Enzimas Inmovilizadas/química , Hidrogenasas/química , Modelos Moleculares , Oxidación-Reducción , Protones , Termodinámica , Viológenos/químicaRESUMEN
Electrostatic interactions between proteins are key factors that govern the association and reaction rate. We spectroscopically determine the second-order reaction rate constant (k) of electron transfer from [NiFe] hydrogenase (H2ase) to cytochrome (cyt) c3 at various ionic strengths (I). The k value decreases with I. To analyze the results, we develop a semi-analytical formula for I dependence of k based on the assumptions that molecules are spherical and the reaction proceeds via a transition state. Fitting of the formula to the experimental data reveals that the interaction occurs in limited regions with opposite charges and with radii much smaller than those estimated from crystal structures. This suggests that local charges in H2ase and cyt c3 play important roles in the reaction. Although the crystallographic data indicate a positive electrostatic potential over almost the entire surface of the proteins, there exists a small region with negative potential on H2ase at which the electron transfer from H2ase to cyt c3 may occur. This local negative potential region is identical to the hypothetical interaction sphere predicted by the analysis. Furthermore, I dependence of k is predicted by the Adaptive Poisson-Boltzmann Solver considering all charges of the amino acids in the proteins and the configuration of H2ase/cyt c3 complex. The calculation reproduces the experimental results except at extremely low I. These results indicate that the stabilization derived from the local electrostatic interaction in the H2ase/cyt c3 complex overcomes the destabilization derived from the electrostatic repulsion of the overall positive charge of both proteins.
Asunto(s)
Grupo Citocromo c/química , Desulfovibrio vulgaris/enzimología , Hidrogenasas/química , Modelos Moleculares , Conformación Proteica , Respiración de la Célula , Grupo Citocromo c/metabolismo , Transporte de Electrón , Electrones , Hidrogenasas/metabolismo , Cinética , Concentración Osmolar , Oxidación-Reducción , Mapas de Interacción de Proteínas , Electricidad EstáticaRESUMEN
To understand electrostatic interactions in biomolecules, the bimolecular rate constants (k) between redox enzymes and charged substrates (in this study, redox mediators in the electrode reaction) were evaluated at various ionic strengths (I) for the mediated bioelectrocatalytic reaction. The k value between bilirubin oxidase (BOD) and positively charged mediators increased with I, while that between BOD and negatively charged mediators decreased with I. The opposite trend was observed for the reaction of glucose oxidase (GOD). In the case of noncharged mediators, the k value was independent of I for both BOD and GOD. These results reflect the electrostatic interactions between the enzymes and the mediators. Furthermore, we estimated k/k° (k° being the thermodynamic rate constant) by numerical simulation (finite element method) based on the Poisson-Boltzmann (PB) equation. By considering the charges of individual atoms involved in the amino acids around the substrate binding sites in the enzymes, the simulated k/k° values well reproduced the experimental data. In conclusion, k/k° can be predicted by PB-based simulation as long as the crystal structure of the enzyme and the substrate binding site are known.
Asunto(s)
Glucosa Oxidasa/química , Glucosa Oxidasa/metabolismo , Simulación de Dinámica Molecular , Oxidorreductasas actuantes sobre Donantes de Grupo CH-CH/química , Oxidorreductasas actuantes sobre Donantes de Grupo CH-CH/metabolismo , Concentración Osmolar , Oxidación-Reducción , Distribución de Poisson , Conformación Proteica , TermodinámicaRESUMEN
Effects of the electrode poential on the activity of an adsorbed enzyme has been examined by using copper efflux oxidase (CueO) as a model enzyme and by monitoring direct electron transfer (DET)-type bioelectrocatalysis of oxygen reduction. CueO adsorbed on bare Au electrodes at around the point of zero charge (E(pzc)) shows the highest DET activity, and the activity decreases as the adsorption potential (E(ad); at which the enzyme adsorbs) is far from E(pzc). We propose a model to explain the phenomena in which the electrostatic interaction between the enzyme and electrodes in the electric double layer affects the orientation and the stability of the adsorbed enzyme. The self-assembled monolayer of butanethiol on Au electrodes decreases the electric field in the outside of the inner Helmholtz plane and drastically diminishes the E(ad) dependence of the DET activity of CueO. When CueO is adsorbed on bare Au electrodes under open circuit potential and then is held at hold potentials (E(ho)) more positive than E(pzc), the DET activity of the CueO rapidly decreases with the hold time. The strong electric field with positive surface charge density on the metallic electrode (σ(M)) leads to fatal denaturation of the adsorbed CueO. Such denaturation effect is not so serious at E(ho)<Asunto(s)
Técnicas Biosensibles
, Catálisis
, Oxidorreductasas/aislamiento & purificación
, Adsorción
, Electricidad
, Transporte de Electrón
, Oro/química
, Oxidorreductasas/química
, Desnaturalización Proteica
, Compuestos de Sulfhidrilo/química
, Propiedades de Superficie