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1.
Front Chem ; 12: 1424548, 2024.
Artículo en Inglés | MEDLINE | ID: mdl-38911994

RESUMEN

The oxalic acid complexation method and sulfuric acid heat treatment method were used to synthesize the YMnO3 (YMO) and YMO-SO4 2- (YMO-SO) photocatalysts. The YMO-SO photocatalyst maintained the crystal structure of YMO, but the particle size increased slightly and the optical band gap decreased significantly. The YMO-SO photocatalyst demonstrates a wide range of light absorption capabilities, covering ultraviolet, visible and near-infrared light. The photocatalytic activity of YMO-SO was investigated with ibuprofen as the target pollutant. The YMO-SO photocatalyst exhibits high ultraviolet (UV), visible and near-infrared photocatalytic activity. Experiments with different environmental parameters confirmed that the best catalyst content was 1 g/L, the best drug concentration was 75 mg/L and the best pH value was 7. The capture experiment, free radical detection experiment and photocatalytic mechanism analysis confirmed that the main active species of YMO-SO photocatalyst were hole and superoxide free radical.

2.
ChemSusChem ; 13(7): 1785-1792, 2020 Apr 07.
Artículo en Inglés | MEDLINE | ID: mdl-31944592

RESUMEN

The development of mild and efficient processes for the selective oxygenation of organic compounds by molecular oxygen (O2 ) is key for the synthesis of oxygenates. This paper discloses an atom-efficient synthesis protocol for the photo-oxygenation of 9,10-dihydroanthracene (DHA) by O2 to anthraquinone (AQ), which could achieve quantitative AQ yield (100 %) without any extra catalysts or additives under ambient temperature and pressure. A yield of 86.4 % AQ was obtained even in an air atmosphere. Furthermore, this protocol showed good compatibility for the photo-oxidation of several other compounds with similar structures to DHA. From a series of control experiments, free-radical quenching, and electron paramagnetic resonance spin-trapping results, the photo-oxygenation of DHA was probably initiated by its photoexcited state DHA*, and the latter could activate O2 to a superoxide anion radical (O2 .- ) through the transfer of its electron. Subsequently, this photo-oxidation was gradually dominated by the oxygenated product AQ as an active photocatalyst obtained from the oxidation of DHA by O2 .- , and was accelerated with the rapid accumulation of AQ. The present photo-oxidation protocol is a good example of selective oxygenation based on the photoexcited substrate self-activated O2 , which complies well with green chemistry ideals.

3.
Redox Biol ; 12: 462-468, 2017 08.
Artículo en Inglés | MEDLINE | ID: mdl-28334681

RESUMEN

Fluorescent proteins are an important tool that has become omnipresent in life sciences research. They are frequently used for localization of proteins and monitoring of cells [1,2]. Green fluorescent protein (GFP) was the first and has been the most used fluorescent protein. Enhanced GFP (eGFP) was optimized from wild-type GFP for increased fluorescence yield and improved expression in mammalian systems [3]. Many GFP-like fluorescent proteins have been discovered, optimized or created, such as the red fluorescent protein TagRFP [4]. Fluorescent proteins are expressed colorless and immature and, for eGFP, the conversion to the fluorescent form, mature, is known to produce one equivalent of hydrogen peroxide (H2O2) per molecule of chromophore [5,6]. Even though it has been proposed that this process is non-catalytic and generates nontoxic levels of H2O2 [6], this study investigates the role of fluorescent proteins in generating free radicals and inducing oxidative stress in biological systems. Immature eGFP and TagRFP catalytically generate the free radical superoxide anion (O2•-) and H2O2 in the presence of NADH. Generation of the free radical O2•- and H2O2 by eGFP in the presence of NADH affects the gene expression of cells. Many biological pathways are altered, such as a decrease in HIF1α stabilization and activity. The biological pathways altered by eGFP are known to be implicated in the pathophysiology of many diseases associated with oxidative stress; therefore, it is critical that such experiments using fluorescent proteins are validated with alternative methodologies and the results are carefully interpreted. Since cells inevitably experience oxidative stress when fluorescent proteins are expressed, the use of this tool for cell labeling and in vivo cell tracing also requires validation using alternative methodologies.


Asunto(s)
Proteínas Fluorescentes Verdes/metabolismo , Peróxido de Hidrógeno/metabolismo , Superóxidos/metabolismo , Catálisis , Células HEK293 , Células HeLa , Humanos , Subunidad alfa del Factor 1 Inducible por Hipoxia/genética , Subunidad alfa del Factor 1 Inducible por Hipoxia/metabolismo , Proteínas Luminiscentes/metabolismo , NAD/metabolismo , Estrés Oxidativo , Proteína Fluorescente Roja
4.
J Biomol Struct Dyn ; 34(3): 475-85, 2016.
Artículo en Inglés | MEDLINE | ID: mdl-25990646

RESUMEN

Enzymes are known to be denatured upon boiling, although Cu,Zn superoxide dismutase of Potentilla atrosanguinea (Pot-SOD) retains significant catalytic activity even after autoclaving (heating at 121 °C at a pressure of 1.1 kg per square cm for 20 min). The polypeptide backbone of Pot-SOD consists of 152 amino acids with a central core spanning His45 to Cys145 that is involved in coordination of Cu(2+) and Zn(2+) ions. While the central core is essential for imparting catalytic activity and structural stability to the enzyme, the role of sequences flanking the central core was not understood. Experiments with deletion mutants showed that the amino acid sequences flanking the central core were important in retaining activity of Pot-SOD after autoclaving. Molecular dynamics simulations demonstrated the unfavorable structure of mutants due to increased size of binding pocket and enhanced negative charge on the electrostatic surface, resulting in unavailability of the substrate superoxide radical ([Formula: see text]) to the catalytic pocket. Deletion caused destabilization of structural elements and reduced solvent accessibility that further produced unfavorable structural geometry of the protein.


Asunto(s)
Aminoácidos/química , Dominio Catalítico , Cobre/química , Superóxido Dismutasa/química , Zinc/química , Activación Enzimática , Modelos Moleculares , Conformación Molecular , Simulación de Dinámica Molecular , Desnaturalización Proteica , Estabilidad Proteica , Eliminación de Secuencia , Relación Estructura-Actividad , Superóxido Dismutasa/genética , Superóxido Dismutasa/metabolismo
5.
Cancer Lett ; 367(2): 157-61, 2015 Oct 28.
Artículo en Inglés | MEDLINE | ID: mdl-26225838

RESUMEN

Chemotherapy-induced cognitive impairment (CICI) is a quality of life-altering consequence of chemotherapy experienced by a large percentage of cancer survivors. Approximately half of FDA-approved anti-cancer drugs are known to produce ROS. Doxorubicin (Dox), a prototypical ROS-generating chemotherapeutic agent, generates superoxide (O2(-)•) via redox cycling. Our group previously demonstrated that Dox, which does not cross the BBB, induced oxidative damage to plasma proteins leading to TNF-α elevation in the periphery and, subsequently, in brain following cancer chemotherapy. We hypothesize that such processes play a central role in CICI. The current study tested the notion that O2(-)• is involved and likely responsible for Dox-induced plasma protein oxidation and TNF-α release. Addition of O2(-)• as the potassium salt (KO2) to plasma resulted in significantly increased oxidative damage to proteins, indexed by protein carbonyl (PC) and protein-bound HNE levels. We then adapted this protocol for use in cell culture. Incubation of J774A.1 macrophage culture using this KO2-18crown6 protocol with 1 and 10 µM KO2 resulted in dramatically increased levels of TNF-α produced. These findings, together with our prior results, provide strong evidence that O2(-)• and its resulting reactive species are critically involved in Dox-induced plasma protein oxidation and TNF-α release.


Asunto(s)
Antibióticos Antineoplásicos/toxicidad , Proteínas Sanguíneas/metabolismo , Trastornos del Conocimiento/inducido químicamente , Doxorrubicina/toxicidad , Macrófagos/efectos de los fármacos , Síndromes de Neurotoxicidad/etiología , Estrés Oxidativo/efectos de los fármacos , Carbonilación Proteica/efectos de los fármacos , Superóxidos/toxicidad , Factor de Necrosis Tumoral alfa/metabolismo , Aldehídos/sangre , Animales , Línea Celular , Trastornos del Conocimiento/sangre , Relación Dosis-Respuesta a Droga , Peroxidación de Lípido/efectos de los fármacos , Macrófagos/metabolismo , Masculino , Ratones , Síndromes de Neurotoxicidad/sangre , Factores de Tiempo , Regulación hacia Arriba
6.
Artículo en Chino | WPRIM (Pacífico Occidental) | ID: wpr-550159

RESUMEN

The effect of maltol to prevent erythrocyte from auto-oxidation is presented. When erythrocytes were incubated at 37 ℃ for 24 h in vitro, oxyhemoglobin was decreased, methemoglobin, superoxide freeradical, lipofuscin and Heinz's body were increased as well as membrane proteins were changed. These reactions could be inhibited by maltol.

7.
Artículo en Chino | WPRIM (Pacífico Occidental) | ID: wpr-554566

RESUMEN

Objective: To study the scavenging capacity of extract from four kinds of barley leaves on superoxide free radical and hydroxyl free radical. Methods: Measure the content of superoxide free radical and hydroxyl free radical by nitro blue tetrazolium(NBT) photo-reduction. Results: Along with the flavonoid in the reaction liquid, the scavenging rate shows ascending trend . When the concentration of flavonoid is 12?g/ml, its scavenging rate is 95.56% and 94.12% on superoxide free radical and hydroxyl free radical respectively. Conclusion: The flavonoids of barley leave s have stronger anti-oxidative action.

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