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Herein, an eco-friendly lignin-based N-doped cocatalyst (N/C) was fabricated to enhance Fenton-like oxidation capacity. The N/ C-assisted Fe(III)/H 2 O 2 system showed ultrafast pollutant oxidation activity via an accelerated Fe(III)/Fe(II) cycle, exhibiting 16.9 times better caffeine removal efficiency than equivalent quantities of the classical Fenton system. N/C cocatalysts exhibited extraordinary stability and generality in the decontamination and disinfection of complex solution matrixes. Both experimental and theoretical calculation results demonstrated that graphitic N was the active site on N/C cocatalysts, which could elevate the reactivity of Fe(III) and make the interfacial electron transfer more feasible. In the N/C-mediated Fe(III)/H 2 O 2 system, an increase in electron transfer on the surface of N/C facilitated the formation of surface-bound Fe(II), thereby activating H 2 O 2 to produce hydroxyl radicals, the main active species for contaminant degradation. Notably, practical continuous water purification could be achieved by assembling N/C into fixed-bed reactors or membrane treatment units. These findings provide novel insights into N-doped carbonaceous cocatalysts and a promising green strategy for practical water treatment.

Rare earth elements (REEs) are critical for numerous modern technologies, and demand is increasing globally; however, production steps are resource-intensive and environmentally damaging. Some plant species are able to hyperaccumulate REEs, and understanding the biology behind this phenomenon could play a pivotal role in developing more environmentally friendly REE recovery technologies. Here, we identified a REE transporter NRAMP REE Transporter 1 (NREET1) from the REE hyperaccumulator fern Dicranopteris linearis. Although NREET1 belongs to the natural resistance-associated macrophage protein (NRAMP) family, it shares a low similarity with other NRAMP members. When expressed in yeast, NREET1 exhibited REE transport capacity, but it could not transport divalent metals, such as zinc, nickel, manganese, or iron. NREET1 is mainly expressed in D. linearis roots and predominantly localized in the plasma membrane. Expression studies in Arabidopsis thaliana revealed that NREET1 functions as a transporter mediating REE uptake and transfer from root cell walls into the cytoplasm. Moreover, NREET1 has a higher affinity for transporting light REEs compared to heavy REEs, which is consistent to the preferential enrichment of light REEs in field-grown D. linearis. We therefore conclude that NREET1 may play an important role in the uptake and consequently hyperaccumulation of REEs in D. linearis. These findings lay the foundation for the use of synthetic biology techniques to design and produce sustainable, plant-based REE recovery systems.

Nutrient uptake by plant roots seriously affects the growth and yield of maize. AUX/IAA encoding genes play an important role in auxin signal transduction and regulating the growth of plant roots.In this study, AUX/IAA gene ZmLLG1 was cloned from maize. The expression level of the ZmLLG1 gene in different tissues was detected by qRT-PCR, and ZmLLG1 was found to be overexpressed in the roots of maize. Arabidopsis thaliana and mutant maize were both analyzed by statistical method. A yeast two-hybrid experiment, BiFC experiment and pull-down experiment were used to verify the interactions between the protein and ZmLLG1.The CoDing Sequence (CDS) of ZmLLG1 is 684 bp and encodes a protein composed of 227 amino acids. A subcellular localization analysis confirmed that ZmLLG1 was localized in the nucleus. The ZmLLG1 gene was expressed in all tissues of maize, but its expression level was highest in the root. The root length and number of lateral roots of zmllg1 mutant maize were much lower than those of wild-type B73 maize, and ZmLLG1 was responsive to auxin. The yeast two-hybrid assay, BiFC experiment and pull-down assay showed that ZmLLG1 could interact with ZmARF5, ZmARF7, and ZmARF25 to regulate the growth and development of the maize root system. Keywords AUX/IAA, Root, ARF, Maize mutant, Protein