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HO Triggering Electron-Directed Transfer of Emerging Contaminants over Asymmetric Nano Zinc Oxide Surfaces for Water Self-Purification Expansion.
JACS Au
January 2025
Key Laboratory for Water Quality and Conservation of the Pearl River Delta, Ministry of Education, Institute of Environmental Research at Greater Bay, Guangzhou University, Guangzhou 510006, China.
Slow mass transfer processes between inert emerging contaminants (ECs) and dissolved oxygen (DO) limit natural water self-purification; thus, excessive energy consumption is necessary to achieve ECs removal, which has become a longstanding global challenge. Here, we propose an innovative water self-purification expansion strategy by constructing asymmetric surfaces that could modulate trace HO as trigger rather than oxidant to bridge a channel between inert ECs and natural dissolved oxygen, achieved through a dual-reaction-center (DRC) catalyst consisting of Cu/Co lattice-substituted ZnO nanorods (CCZO-NRs). During water purification, the bond lengths of emerging contaminants (ECs) adsorbed on the asymmetric surface were stretched, and this stretching was further enhanced by HO mediation, resulting in a significant reduction of bond-breaking energy barriers.
View Article and Find Full Text PDFRational pore engineering reveals the relative contribution of enzymatic sites and self-assembly towards rapid ferroxidase activity and mineralization: impact of electrostatic guiding and cage-confinement in bacterioferritin.
Chem Sci
January 2025
Department of Chemistry, National Institute of Technology Rourkela - 769008 Odisha India +91-661-2462651 +91-661-2462980.
The self-assembled ferritin protein nanocage plays a pivotal role during oxidative stress, iron metabolism, and host-pathogen interaction by executing rapid iron uptake, oxidation and its safe-storage. Self-assembly creates a nanocompartment and various pores/channels for the uptake of charged substrates (Fe) and develops a concentration gradient across the protein shell. This phenomenon fuels rapid ferroxidase activity by an upsurge in the substrate concentration at the catalytic sites.
View Article and Find Full Text PDFLine-Shifting Triarylmethyl Radicals for Imaging of Enzyme Activity Using Overhauser-Enhanced Magnetic Resonance Imaging: Application to Alkaline Phosphatase.
Chem Biomed Imaging
January 2025
In Vivo Multifunctional Magnetic Resonance Center, Robert C. Byrd Health Sciences Center, West Virginia University, Morgantown, West Virginia 26506, United States.
Enzyme catalytic activities are critical biomarkers of tissue states under physiological and pathophysiological conditions. However, the direct measurement and imaging of enzyme activity remains extremely challenging. We report the synthesis and characterization of the first stable triarylmethyl (TAM) radical substrate of alkaline phosphatase (TAM-ALPs).
View Article and Find Full Text PDFDirected evolution of peroxidase DNAzymes by a function-based approach.
Biol Methods Protoc
December 2024
School of Biomedical Sciences, LKS Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, P.R. China.
Peroxidase DNAzymes are single-stranded, stable G-quadruplexes structures that exhibit catalytic activity with cofactor hemin. This class of DNAzymes offers several advantages over traditional protein and RNA catalysts, including thermal stability, resistance to hydrolysis, and easy of synthesis in the laboratory. However, their use in medicine, biology, and chemistry is limited due to their low catalytic rates.
View Article and Find Full Text PDFTotal Synthesis of Dixiamycins A and B via a Late-Stage N-N Bond Formation under Visible Light Photoredox Catalysis.
Org Lett
January 2025
Department of Chemistry, Indian Institute of Science Education and Research Bhopal, Bhauri, Bhopal 462066, Madhya Pradesh, India.
Intermolecular oxidative N-N bond formation reactions are quite challenging and are largely uncharted. N-N linked dimeric indolosesquiterpene alkaloids represent an underexplored class of natural products, and strategies for direct dehydrogenative N-N bond formation are limited. Here, we have reported that a late-stage visible-light photoredox catalysis facilitates N-N bond formation, leading to the total syntheses of atropo-diastereomers dixiamycins A () and B ().
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