Numerous applications have been described for microperoxidases (MPs) such as in photoreceptors, sensing, drugs, and hydrogen evolution. The last application was obtained by replacing Fe(III), the native central metal, by cobalt ion and inspired part of the present study. Here, the Fe(III) of MP-11 was replaced by Cu(II) that is also a stable redox state in aerated medium, and the structure and activity of both MPs were modulated by the interaction with the positively charged interfaces of lipids. Comparative spectroscopic characterization of Fe(III) and Cu(II)MP-11 in the studied media demonstrated the presence of high and low spin species with axial distortion. The association of the Fe(III)MP-11 with CTAB and Cu(II)MP-11 with DODAB affected the colloidal stability of the surfactants that was recovered by heating. This result is consistent with hydrophobic interactions of MPs with DODAB vesicles and CTAB micelles. The hydrophobic interactions decreased the heme accessibility to substrates and the Fe(III) MP-11catalytic efficiency. Cu(II)MP-11 challenged by peroxides exhibited a cyclic Cu(II)/Cu(I) interconversion mechanism that is suggestive of a mimetic Cu/ZnSOD (superoxide dismutase) activity against peroxides. Hydrogen peroxide-activated Cu(II)MP-11 converted Amplex Red to dihydroresofurin. This study opens more possibilities for technological applications of MPs.
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http://dx.doi.org/10.3390/molecules22081212 | DOI Listing |
Sci Rep
January 2025
Department of Physics, Faculty of Science, Fasa University, Fasa, 74616-86131, Iran.
In this work, we explored the role of a single electron in the energy of neutral and charged clusters of using data visualization and statistical techniques as a new insight. Initially, we studied the effects of one electron, time, and temperature on energy using multiple linear regression analysis with dummy variables, and the results demonstrated that all three predictors significantly affected the energy. Time had a positive impact (direct ratio effect) on the energy of , and and a negative impact (inverse ratio effect) on the energy of while temperature had a positive effect on the energy of all three sodium clusters.
View Article and Find Full Text PDFEnviron Res
January 2025
School of Chemical Engineering, Zhengzhou University, Zhengzhou 450001, China; Zhongyuan Critical Metals Laboratory, Zhengzhou University, Zhengzhou 450001, China; The Key Lab of Critical Metals Minerals Supernormal Enrichment and Extraction, Ministry of Education, Zhengzhou 450001, China.
Given the environmental and ecological risks posed by wastewater bearing Mo, the characteristics and microscopic interactions of existing silica-based adsorbents have not been thoroughly investigated, highlighting the need to enhance the porosity and chemical interactions of these materials. Considering the effectiveness of amino groups in binding metal oxyanions, this study investigates the adsorption performance and mechanism of amino-functionalized MCM-41 for Mo(VI), with the goal of efficiently remediating Mo-contaminated wastewater. MCM-41 modified by amino group retains its original structure and mesoporous characteristics while featuring a positively charged surface and chemically bonded amino groups.
View Article and Find Full Text PDFTalanta
January 2025
College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, No. 30, Puzhu South Road, Nanjing, 211816, China; State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, No. 30, Puzhu South Road, Nanjing, 211816, China. Electronic address:
Enzyme immobilization techniques are crucial for enhancing enzyme stability and catalytic efficiency. Traditional methods such as physical adsorption and simple covalent binding often fail to maintain enzyme activity and stability. In this study, an innovative multi-level immobilization strategy was proposed to achieve efficient targeted immobilization of nuclease P1 (NP1) by fine-tuning the surface microenvironment.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Research Unit on Computational Biology and Drug Design, Children's Hospital of Mexico Federico Gómez, Mexico City 06720, Mexico.
Cell-penetrating peptides (CPPs) are a diverse group of peptides, typically composed of 4 to 40 amino acids, known for their unique ability to transport a wide range of substances-such as small molecules, plasmid DNA, small interfering RNA, proteins, viruses, and nanoparticles-across cellular membranes while preserving the integrity of the cargo. CPPs exhibit passive and non-selective behavior, often requiring functionalization or chemical modification to enhance their specificity and efficacy. The precise mechanisms governing the cellular uptake of CPPs remain ambiguous; however, electrostatic interactions between positively charged amino acids and negatively charged glycosaminoglycans on the membrane, particularly heparan sulfate proteoglycans, are considered the initial crucial step for CPP uptake.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Medicines Discovery Institute, Cardiff University, Cardiff CF10 3AT, UK.
DNA gyrase is a bacterial type IIA topoisomerase that can create temporary double-stranded DNA breaks to regulate DNA topology and an archetypical target of antibiotics. The widely used quinolone class of drugs use a water-metal ion bridge in interacting with the GyrA subunit of DNA gyrase. Zoliflodacin sits in the same pocket as quinolones but interacts with the GyrB subunit and also stabilizes lethal double-stranded DNA breaks.
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