Biodegradation of hexabromocyclododecane by Rhodopseudomonas palustris YSC3 strain: A free-living nitrogen-fixing bacterium isolated in Taiwan.

The persistent organic pollutant, brominated flame retardant, hexabromocyclododecane (HBCD), identified as an emerging contaminant has been detected in various environmental matrix. The increased level of this toxic organic compound in the environment has been associated with serious human health risks. The results obtained from this study revealed that various Rhodopseudomonas palustris strains isolated from paddy soil in Taiwan possessed good HBCD biodegradation capability when they were cultured aerobically. Among these strains, YSC3 was considered as one of the most potential isolates for HBCD degradation. The optimum HBCD biodegradation occurred at neutral pH and at 35 °C in all our pH and temperature tests at an initial HBCD concentration of 1 ppm. HBCD degradation kinetics generally decreased with the increase of initial HBCD concentration. The study also suggested that the cultivation temperature played a vital role on YSC3 for its initiation of cellular HBCD degradation. The relative-molar ratio of the released bromide ions during the biodegradation of HBCD was observed in the range between 1 and 3.5, suggesting that the debromination reactions occurred. Concomitant with the loss of HBCD, there was a concurrent production of two metabolites, pentabromocyclododecanol and pentabromocyclododecene, which were determined by liquid chromatography and mass spectrometry techniques. On the basis of the obtained results, the possible biodegradation pathways were also proposed in this study.

Functional characterization of ECP-heparin interaction: a novel molecular model.

Human eosinophil cationic protein (ECP) and eosinophil derived neurotoxin (EDN) are two ribonuclease A (RNaseA) family members secreted by activated eosinophils. They share conserved catalytic triad and similar three dimensional structures. ECP and EDN are heparin binding proteins with diverse biological functions. We predicted a novel molecular model for ECP binding of heparin hexasaccharide (Hep6), [GlcNS(6S)-IdoA(2S)]3, and residues Gln(40), His(64) and Arg(105) were indicated as major contributions for the interaction. Interestingly, Gln(40) and His(64) on ECP formed a clamp-like structure to stabilize Hep6 in our model, which was not observed in the corresponding residues on EDN. To validate our prediction, mutant ECPs including ECP Q40A, H64A, R105A, and double mutant ECP Q40A/H64A were generated, and their binding affinity for heparins were measured by isothermal titration calorimetry (ITC). Weaker binding of ECP Q40A/H64A of all heparin variants suggested that Gln(40)-His(64) clamp contributed to ECP-heparin interaction significantly. Our in silico and in vitro data together demonstrate that ECP uses not only major heparin binding region but also use other surrounding residues to interact with heparin. Such correlation in sequence, structure, and function is a unique feature of only higher primate ECP, but not EDN.