Antimony (Sb) is a toxic metalloid, and its pollution has become a global environmental problem as a result of its extensive use and corresponding Sb-mining activities. The toxicity and mobility of Sb strongly depend on its chemical speciation. In this review, we summarize the current knowledge on the biogeochemical processes (including emission, distribution, speciation, redox, metabolism and toxicity) that trigger the mobilization and transformation of Sb from pollution sources to the surrounding environment. Natural phenomena such as weathering, biological activity and volcanic activity, together with anthropogenic inputs, are responsible for the emission of Sb into the environment. Sb emitted in the environment can adsorb and undergo redox reactions on organic or inorganic environmental media, thus changing its existing form and exerting toxic effects on the ecosystem. This review is based on a careful and systematic collection of the latest papers during 2010-2017 and our research results, and it illustrates the fate and ecological effects of Sb in the environment.

Antimony speciation in the environment: Recent advances in understanding the biogeochemical processes and ecological effects

Antimony contamination and its risk management in complex environmental settings: A review

Agrobacterium-mediated horizontal gene transfer: Mechanism, biotechnological application, potential risk and forestalling strategy.

Impacts of antimony and arsenic co-contamination on the river sedimentary microbial community in an antimony-contaminated river

Some arsenite [As(III)]-oxidizing bacteria exhibit positive chemotaxis towards As(III), however, the related As(III) chemoreceptor and regulatory mechanism remain unknown. The As(III)-oxidizing bacterium Agrobacterium tumefaciens GW4 displays positive chemotaxis towards 0.5-2 mM As(III). Genomic analyses revealed a putative chemoreceptor-encoding gene, mcp, located in the arsenic gene island and having a predicted promoter binding site for the As(III) oxidation regulator AioR. Expression of mcp and other chemotaxis related genes (cheA, cheY2 and fliG) was inducible by As(III), but not in the aioR mutant. Using capillary assays and intrinsic tryptophan fluorescence spectra analysis, Mcp was confirmed to be responsible for chemotaxis towards As(III) and to bind As(III) (but not As(V) nor phosphate) as part of the sensing mechanism. A bacterial one-hybrid system technique and electrophoretic mobility shift assays showed that AioR interacts with the mcp regulatory region in vivo and in vitro, and the precise AioR binding site was confirmed using DNase I foot-printing. Taken together, these results indicate that this Mcp is responsible for the chemotactic response towards As(III) and is regulated by AioR. Additionally, disrupting the mcp gene affected bacterial As(III) oxidation and growth, inferring that Mcp may exert some sort of functional connection between As(III) oxidation and As(III) chemotaxis.

/pdf/arsenite-oxidation-regulator-aior-regulates-bacterial-3j1uoiaf6e.pdf

Arsenite oxidation regulator AioR regulates bacterial chemotaxis towards arsenite in Agrobacterium tumefaciens GW4.

Previously, we found that arsenite (AsIII) oxidation could improve the generation of ATP/NADH to support the growth of Agrobacterium tumefaciens GW4. In this study, we found that aioE is induced by AsIII and located in the arsenic island near the AsIII oxidase genes aioBA and co-transcripted with the arsenic resistant genes arsR1-arsC1-arsC2-acr3-1. AioE belongs to TrkA family corresponding the electron transport function with the generation of NADH and H+. An aioE in-frame deletion strain showed a null AsIII oxidation and a reduced AsIII resistance, while a cytC mutant only reduced AsIII oxidation efficiency. With AsIII, aioE was directly related to the increase of NADH, while cytC was essential for ATP generation. In addition, cyclic voltammetry analysis showed that the redox potential (ORP) of AioBA and AioE were +0.297 mV vs. NHE and +0.255 mV vs. NHE, respectively. The ORP gradient is AioBA > AioE > CytC (+0.217 ~ +0.251 mV vs. NHE), which infers that electron may transfer from AioBA to CytC via AioE. The results indicate that AioE may act as a novel AsIII oxidation electron transporter associated with NADH generation. Since AsIII oxidation contributes AsIII detoxification, the essential of AioE for AsIII resistance is also reasonable.

/pdf/an-oxidoreductase-aioe-is-responsible-for-bacterial-arsenite-252p1i0efl.pdf

An Oxidoreductase AioE is Responsible for Bacterial Arsenite Oxidation and Resistance.

A Gram-staining negative, aerobic, non-motile, rod-shaped bacterial strain, designated YS-37T, was isolated from soil in a manganese factory, People’s Republic of China. Based on16S rRNA gene sequence analysis, strain YS-37T was most closely related to Lysobacter pocheonensis Gsoil 193T (97.0%), Lysobacter dokdonensis DS-58T (96.0%) and Lysobacter daecheongensis Dae08T (95.8%) and grouped together with L. pocheonensis Gsoil 193T and Lysobacter dokdonensis DS-58T. The DNA–DNA hybridization value between strain YS-37T and L. pocheonensis KCTC 12624T was 43.3% (± 1). The major respiratory quinone of strain YS-37T was ubiquinone-8, and the polar lipids were diphosphatidylglycerol, phosphatidylethanolamine, phosphatidylglycerol, phospholipid, phosphatidylmethylethaolamine and two unknown lipids. Its major cellular fatty acids (> 5%) were iso-C15:0, iso-C17:1
 ω9c, iso-C16:0, iso-C11:0 3-OH and iso-C11:0 and the G + C content of the genomic DNA was 67.1 mol%. Strain YS-37T also showed some biophysical and biochemical differences with the related strains, especially in hydrolysis of casein. The results demonstrated that strain YS-37T belongs to genus Lysobacter and represents a novel Lysobacter species for which the name Lysobacter tongrenensis sp. nov. is proposed. The type strain is YS-37T (= CCTCC AB 2016052T = KCTC 52206T).

Lysobacter tongrenensis sp. nov., isolated from soil of a manganese factory.

A Gram-stain-positive, strictly aerobic, non-motile and rod-shaped bacterial strain, designated YS-17T, was isolated from soil in the Lengshuijiang antimony mine, Hunan Province, China. Comparative 16S rRNA gene sequencing analysis clustered it with Flavihumibacter strains, and strain YS-17T was most closely related to Flavihumibacter cheonanensis WS16T (97.2 % similarity), Flavihumibacter petaseus T41T (96.6 %) and Flavihumibacter solisilvae 3-3T (96.5 %). The level of DNA-DNA relatedness between strain YS-17T and F. cheonanensis JCM 19322T was 35.5±0.1 % (n=2). The major respiratory quinone of strain YS-17T was menaquinone-7 and the major polar lipids were phosphatidylethanolamine, two unidentified lipids, two unidentified amino lipids and phospholipid. The major fatty acids (≥5 %) were iso-C15 : 0, iso-C15 : 1 G, unknown ECL 13.565, iso-C17 : 0 3-OH, C15 : 0, C16 : 1ω5c and anteiso-C15 : 0. The DNA G+C content was 47.8 mol%. Compared with other Flavihumibacter strains, strain YS-17T showed major biophysical and biochemical differences, with the ability to hydrolyse gelatin and to assimilate salicin and l-proline. The results demonstrated that strain YS-17T belongs to the genus Flavihumibacter and represents a novel species, for which the name Flavihumibacter stibioxidans sp. nov. is proposed. The type strain is YS-17T (=CCTCC AB 2016053T=KCTC 52205T).

Flavihumibacter stibioxidans sp. nov., an antimony-oxidizing bacterium isolated from antimony mine soil.

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Arsenite oxidation regulator AioR regulates bacterial chemotaxis towards arsenite in Agrobacterium tumefaciens GW4.

An Oxidoreductase AioE is Responsible for Bacterial Arsenite Oxidation and Resistance.

Lysobacter tongrenensis sp. nov., isolated from soil of a manganese factory.

Flavihumibacter stibioxidans sp. nov., an antimony-oxidizing bacterium isolated from antimony mine soil.