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Purification, molecular characterization and metabolic mechanism of an aerobic tetrabromobisphenol A dehalogenase, a key enzyme of halorespiration in Ochrobactrum sp. T
- Liang, Zhishu, Li, Guiying, Xiong, Jukun, Mai, Bixian, An, Taicheng
- Chemosphere 2019 v.237 pp. 124461
- NADP (coenzyme), Ochrobactrum, aerobic conditions, biochemical pathways, bioremediation, bromination, dehalogenation, enzymes, genes, metabolites, molecular weight, paraquat
- Due to the detoxification of tetrabromobisphenol A (TBBPA) varies from different bacterial strains and depends on their specific enzymatic machinery, it is necessary to understand them for potential in situ bioremediation application. The special ability of our previously isolated Ochrobactrum sp. T to simultaneously debrominate and aerobic mineralize TBBPA urgent us to continuously study its degradation molecular mechanism. Herein, the purification and characterization of the dehalogenase which can debrominate TBBPA was investigated based on its corresponding encoding gene tbbpaA. Results showed that an enzyme with molecular mass of 117 kDa, Km of 26.6 μM and Vmax of 0.133 μM min−1 mg−1 was purified and designated as bromophenol dehalogenase. It was the only detected dehalogenase which exhibited TBBPA degradation ability (78%). Moreover, its activity was significantly enhanced by adding NADPH or methyl viologen to the reaction solution. The high similarity of substrate spectrum between the dehalogenase from the recombinant strain and the wild strain further indicated that it was the main dehalogenase responsible for the debromination in wild strain. Based on three identified metabolites, a metabolic pathway of TBBPA by purified enzyme under oxic condition was proposed. This study provides an excellent dehalogenase candidate for mechanistic study of aerobic dehalogenation of brominated aromatic compound.