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Neonicotinoid insecticide pollution in soil and water poses serious environmental risks. Microbial biodegradation is an important neonicotinoid insecticide degradation pathway in the environment. In this study, 70.0% of the acetamiprid in a 200 mg/L solution was degraded by actinomycetes Streptomyces canus CGMCC 13662 (isolated from soil) in 48 h, and the acetamiprid degradation half-life was 27.7 h. Acetamiprid was degraded to IM-1-2 ((E)-1-(1-(((6chloropyridin-3-yl)methyl)(methyl) amino)ethylidene)urea) through hydrolysis of the cyanoimine moiety. Gene cloning and overexpression indicated that a novel nitrile hydratase with three unusual subunits (AnhD, AnhE, and AnhA) without accessory protein mediated IM-1-2 formation. The purified nitrile hydratase responsible for degrading acetamiprid had a K m of 5.85 mmol/L and a V max of 15.99 U/mg. A homology model suggested that AnhD-Glu56 and AnhE-His21 play important roles in the catalytic efficiency of the nitrile hydratase. S. canus CGMCC 13662 could be used to remediate environments contaminated with acetamiprid.

is a metabolically diverse genus of plant growth-promoting rhizobacteria (PGPR) that engages in mutually beneficial interactions between plants and microbes. Unlike most PGPR, cannot synthesize the phytohormone indole-3-acetic acid (IAA) via tryptophan. However, we found that strain CGMCC 4969 can produce IAA using indole-3-acetonitrile (IAN) as the precursor. Thus, in the present study, the IAA synthesis mechanism of CGMCC 4969 was investigated. CGMCC 4969 metabolized IAN to IAA through both a nitrilase-dependent pathway and a nitrile hydratase (NHase) and amidase-dependent pathway. Cobalt enhanced the metabolic flux via the NHase/amidase, by which IAN was rapidly converted to indole-3-acetamide (IAM) and in turn to IAA. IAN stimulated metabolic flux via the nitrilase, by which IAN was rapidly converted to IAA. Subsequently, the IAA was degraded. CGMCC 4969 can use IAN as the sole carbon and nitrogen source for growth. Genome sequencing confirmed the IAA synthesis pathways. Gene cloning and overexpression in indicated that NitA has nitrilase activity and IamA has amidase activity to respectively transform IAN and IAM to IAA. Interestingly, NitA showed a close genetic relationship with the nitrilase of the phytopathogen Quantitative PCR analysis indicated that the NHase/amidase system is constitutively expressed, whereas the nitrilase is inducible. The present study helps our understanding of the versatile functions of nitrile-converting enzymes that mediate IAA synthesis and the interactions between plants and these bacteria. We demonstrated that CGMCC 4969 has two enzymatic systems-nitrilase and nitrile hydratase/amidase-that convert indole-3-acetonitrile (IAN) to the important plant hormone indole-3-acetic acid (IAA). The two IAA synthesis systems have very different regulatory mechanisms, affecting the IAA synthesis rate and duration. The nitrilase was induced by IAN, which was rapidly converted to IAA; subsequently, IAA was rapidly consumed for cell growth. The nitrile hydratase (NHase) and amidase system was constitutively expressed and slowly but continuously synthesized IAA. In addition to synthesizing IAA from IAN, CGMCC 4969 has a rapid IAA degradation system, which would be helpful for a host plant to eliminate redundant IAA. This study indicates that the plant growth-promoting rhizobacterium CGMCC 4969 has the potential to be used by host plants to regulate the IAA level.

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Herein, an anionic metal-organic framework, formulated as {[Zn3(OH)(bmipia)(H2O)3]4·[Zn(H2O)6.5]2}n (FCS-3), was prepared from zinc ions and semi-rigid carboxylate ligands 5-[N, N-bis(5-methylisophthalic acid)amion] isophthalic acid (H6bmipia) and was employed as a unique...

The design and construction of efficient artificial enzyme-mimicking nanomaterials, nanozymes, is highly desirable because of their high stability and low cost. Recent studies have demonstrated iron oxide nanomaterials as multifunctional nanozymes. However, the catalytic mechanism remains unclear. Herein we have combined density functional theory calculations with microkinetic modeling to demonstrate (Fe 3 O 4 ) n (n = 1 to 2) exhibiting the intrinsic activity of mimicking enzymes of catalases (CATs), superoxide dismutases (SODs), and peroxidases (PODs). Their catalytic activities are facilitated by the close proximity of undercoordinated, tunable Fe/O pairs on the (Fe 3 O 4 ) n surfaces. The (Fe 3 O 4 ) n (n = 1 to 2) with different morphologies and sizes exhibited different catalytic activities on the order of Fe 3 O 4 > (Fe 3 O 4 ) 2 . Three possible reaction mechanisms of CAT-like activity (i.e., base-like dissociative mechanism, acid-like dissociative mechanism, and bihydrogen peroxide associative mechanism) and two possible reaction mechanisms of SOD-like activity (i.e., Langmuir−Hinshelwood mechanism and Eley−Rideal mechanism) are systematically explored based on minimum energy path calculations. It is identified that the acid-like dissociative mechanism and the Langmuir−Hinshelwood mechanism are the energetically most favorable pathways, which is proved by the analysis of the ratedetermining step, the energetic span model, and the rate constant. The degree of turnover frequency control (X TOF ) of the species in the mechanism is calculated and identifies the rate-controlling intermediates and transition states (i.e., those with the highest X TOF ), which are used as descriptors to modify and improve the (Fe 3 O 4 ) n catalysts. This study should not only aid our understanding of Fe 3 O 4 artificial enzymes from atomic level but also facilitate the design and construction of other types of target-specific artificial enzymes.

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