Microbial processes are crucial in the redox transformations of toxic selenium oxyanions. This study focused on isolating an efficient selenate-reducing strain, Azospira sp. A9D-23B, and evaluating its capability to recover extracellular selenium nanoparticles (SeNPs) from selenium-laden wastewater in different reactor setups. Analysis using transmission electron microscopy (TEM) and energy-dispersive X-ray spectroscopy (EDX) revealed significantly higher extracellular SeNPs production (99%) on the biocathode of the bioelectrochemical (BEC) reactor compared to the conventional bioreactor (65%). Further investigations into the selenate reductase activity of strain A9D-23B revealed distinct mechanisms of selenate reduction in BEC and conventional bioreactor settings. Notably, selenate reductases associated with the outer membrane and periplasm displayed higher activity (18.31 ± 3.8 µmol/mg-min) on the BEC reactor's biocathode compared to the upflow anaerobic conventional bioreactor (3.24 ± 2.9 µmol/mg-min). Conversely, the selenate reductases associated with the inner membrane and cytoplasm exhibited lower activity (5.82 ± 2.2 µmol/mg-min) on the BEC reactor's biocathode compared to the conventional bioreactor (9.18 ± 1.6 µmol/mg-min). However, the comparable kinetic parameter (K_m) across cellular fractions in both reactors suggest that SeNPs localization was influenced by enzyme activity rather than selenate affinity. Overall, the mechanism involved in selenate reduction to SeNPs and the strain's efficiency in detoxifying selenate below levels regulated by U.S. Environmental Protection Agency have broad implications for sustainable environmental remediation strategies.
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This content will become publicly available on January 10, 2026
CpgD is a phosphoglycerate cytidylyltransferase required for ceramide diphosphoglycerate synthesis
Abstract Lipopolysaccharide (LPS) is essential in most Gram-negative bacteria, but mutants of several species have been isolated that can survive in its absence.Caulobacter crescentusviability in the absence of LPS is partially dependent on the anionic sphingolipid ceramide diphosphoglycerate (CPG2). Genetic analyses showed thatccna_01210, which encodes a nucleotidyltransferase, is required for CPG2 production. Using purified recombinant protein, we determined that CCNA_01210 (CpgD) is a phosphoglycerate cytidylyltransferase which uses CTP and 3-phosphoglycerate to produce CDP-glycerate, which we hypothesize is the phosphoglycerate donor for CPG2 synthesis. CpgD had optimum activity at pH 7.5-8 in the presence of magnesium. CpgD exhibited Michaelis-Menten kinetics with respect to 3-phosphoglycerate (Km,app = 10.9 ± 0.7 mM; Vmax,app = 0.72 ± 0.02 µmol/min/mg enzyme) and CTP (Km,app = 4.8 ± 0.9 mM; Vmax,app = 0.44 ± 0.03 µmol/min/mg enzyme). The characterization of this enzyme uncovers another piece of the pathway towards CPG2 synthesis.
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- Award ID(s):
- 2224195
- PAR ID:
- 10589878
- Publisher / Repository:
- bioRxiv
- Date Published:
- Format(s):
- Medium: X
- Institution:
- bioRxiv
- Sponsoring Org:
- National Science Foundation
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