Generation of active Co(III) and peroxodiphosphate by synergistic electrocatalytic system with phosphate and the mediator cobalt(II) and its degradation performance.

The promising synergistic electrocatalytic system of phosphate (PO43-) with the mediator cobalt(II) (for short E-Co(II)-PO43-) was employed to degrade cationic dye methylene blue (MB). The exploration in the electrocatalytic process revealed that the main intermediate active oxidation products were Co(III), accompanied with hydroxyl radicals and peroxodiphosphates (P2O84-). Their synergistic electrocatalytic degradation rate to MB and total organic carbon (TOC) was up to 100 and 60% in 40 min, respectively, which was 5 times and 2.6 times that in a direct electrocatalytic system, correspondingly. The degradation process of the E-Co(II)-PO43- system on MB started with the bond being broken at the N-C junction of the MB molecule and intermediate active oxidation substances being generated, such as phenothiazine, 2-amino-5-(N-methylformamide) benzene sulfonic acid and N1,N1-dimethyl-1,4 diaminobenzene. Then, the intermediates were degraded into aniline, phenol and benzene sulfonic acid, and eventually decomposed into inorganic substances like CO2 and water. The electrocatalytic degradation mechanism of E-Co(II)-PO43- system on MB was the combination of indirect oxidation of the intermediate oxidants like Co(III), P2O84- and the hydroxyl radical with direct electrocatalysis on the platinum titanium electrode, where the electrocatalytic oxidation of Co(III) was dominant.

Identification of potential nucleomodulins of Mycoplasma bovis by direct biotinylation and proximity-based biotinylation approaches.

Mycoplasma bovis (M. bovis) is a significant bovine pathogen associated with various diseases, including bovine bronchopneumonia and mastitis resulting in substantial economic losses within the livestock industry. However, the development of effective control measures for M. bovis is hindered by a limited understanding of its virulence factors and pathogenesis. Nucleomodulins are newly identified secreted proteins of bacteria that internalize the host nuclei to regulate host cell gene expression and serve as critical virulence factors. Although recent reports have initiated exploration of mycoplasma nucleomodulins, the efficiency of conventional techniques for identification is very limited. Therefore, this study aimed to establish high-throughput methods to identify novel nucleomodulins of M. bovis. Using a direct biotinylation (DB) approach, a total of 289 proteins were identified including 66 high abundant proteins. In parallel, the use of proximity-based biotinylation (PBB), identified 28 proteins. Finally, seven nucleomodulins were verified to be nuclear by transfecting the bovine macrophage cell line BoMac with the plasmids encoding EGFP-fused proteins and observed with Opera Phenix, including the known nucleomodulin MbovP475 and six novel nucleomodulins. The novel nucleomodulins were four ribosomal proteins (MbovP599, MbovP678, MbovP710, and MbovP712), one transposase (MbovP790), and one conserved hypothetical protein (MbovP513). Among them, one unique nucleomodulin MbovP475 was identified with DB, two unique nucleomodulins (MbovP513 and MbovP710) with PBB, and four nucleomodulins by both. Overall, these findings established a foundation for further research on M. bovis nucleomodulin-host interactions for identification of new virulence factors.