Satellite precipitation products from the Global Precipitation Measurement (GPM) mission and its predecessor the Tropical Rainfall Measuring Mission (TRMM) are a critical data source for hydrological applications in ungauged basins. This study conducted an initial and early evaluation of the performance of the Integrated Multi-satellite Retrievals for GPM (IMERG) final run and the TRMM Multi-satellite Precipitation Analysis 3B42V7 precipitation products, and their feasibility in streamflow simulations in the Chindwin River basin, Myanmar, from April 2014 to December 2015 was also assessed. Results show that, although IMERG and 3B42V7 can potentially capture the spatiotemporal patterns of historical precipitation, the two products contain considerable errors. Compared with 3B42V7, no significant improvements were found in IMERG. Moreover, 3B42V7 outperformed IMERG at daily and monthly scales and in heavy rain detections at four out of five gauges. The large errors in IMERG and 3B42V7 distinctly propagated to streamflow simulations via the Xinanjiang hydrological model, with a significant underestimation of total runoff and high flows. The bias correction of the satellite precipitation effectively improved the streamflow simulations. The 3B42V7-based streamflow simulations performed better than the gauge-based simulations. In general, IMERG and 3B42V7 are feasible for use in streamflow simulations in the study area, although 3B42V7 is better suited than IMERG.
Degradation of toxins by microorganisms is a promising approach for detoxification of agricultural products. Here, a bacterial strain, Sphingomonas S3-4, that has the ability to degrade the mycotoxin deoxynivalenol (DON) was isolated from wheat fields. Incubation of Fusarium-infected wheat grains with S3-4 completely eliminated DON. In S3-4 DON is catabolized into compounds with no detectable phytotoxicity, 3-oxo-DON and 3-epi-DON, via two sequential reactions. Comparative analysis of genome sequences from two DON-degrading strains, S3-4 and Devosia D17, and one non-DON-degrading strain, Sphingobium S26, combined with functional screening of a S3-4 genomic BAC library led to the discovery that a novel aldo/keto reductase superfamily member, AKR18A1, is responsible for oxidation of DON into 3-oxo-DON. DON-degrading activity is completely abolished in a mutant S3-4 strain where the AKR18A1 gene is disrupted. Recombinant AKR18A1 protein expressed in Escherichia coli catalyzed the reversible oxidation/reduction of DON at a wide range of pH values (7.5 to 11) and temperatures (10 to 50 °C). The S3-4 strain and recombinant AKR18A1 also catabolized zearalenone and the aldehydes glyoxal and methyglyoxal. The S3-4 strain and the AKR18A1 gene are promising agents for the control of Fusarium pathogens and detoxification of mycotoxins in plants and in food/feed products.
The cholinesterases, acetylcholinesterase (AChE) and butyrylcholinesterase, are primary targets of organophosphates (OPs). Exposure to OPs can lead to serious cardiovascular complications, respiratory compromise, and death. Current therapy to combat OP poisoning involves an oxime reactivator (2-PAM, obidoxime, TMB4, or HI-6) combined with atropine and on occasion an anticonvulsant. Butyrylcholinesterase, administered in the plasma compartment as a bio-scavenger, has also shown efficacy but is limited by its strict stoichiometric scavenging, slow reactivation, and a propensity for aging. Here, we characterize 10 human (h) AChE mutants that, when coupled with an oxime, give rise to catalytic reactivation and aging resistance of the soman conjugate. With the most efficient human AChE mutant Y337A/F338A, we show enhanced reactivation rates for several OP-hAChE conjugates compared with wild-type hAChE when reactivated with HI-6 (1-(2-hydroxyiminomethyl-1-pyridinium)-3-(4-carbamoyl-1-pyridinium)). In addition, we interrogated an 840-member novel oxime library for reactivation of Y337A/F338A hAChE-OP conjugates to delineate the most efficient oxime-mutant enzyme pairs for catalytic bioscavenging. Combining the increased accessibility of the Y337A mutation to oximes within the space-impacted active center gorge with the aging resistance of the F338A mutation provides increased substrate diversity in scavenging potential for agingprone alkyl phosphate inhibitors.
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