Biomimetic synthesis of selenium nanoparticles by Pseudomonas aeruginosa ATCC 27853: An approach for conversion of selenite

Kora, Aruna Jyothi; Rastogi, Lori

doi:10.1016/j.jenvman.2016.06.029

Cited by 115 publications

(46 citation statements)

References 27 publications

(46 reference statements)

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“…The capability of reducing selenate and selenite in the environment seems to be widespread in the microbial world, as evidenced by the diversity of species (both anaerobic and aerobic) that display this reducing ability. These species include, among others, Pseudomonas stutzeri, Pseudomonas fluorescens 1113, Pseudomonas aeruginosa 17, Duganella sp ., Agrobacterium sp 18, . Enterobacter cloacae 19, Bacillus selenitireducens 20, Azospirillum brasilense 21, Thauera selenatis 22, Azoarcus sp 23.…”

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Production of selenium nanoparticles in Pseudomonas putida KT2440

Avendaño

Chaves

Fuentes

et al. 2016

Sci Rep

107

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Selenium (Se) is an essential element for the cell that has multiple applications in medicine and technology; microorganisms play an important role in Se transformations in the environment. Here we report the previously unidentified ability of the soil bacterium Pseudomonas putida KT2440 to synthesize nanoparticles of elemental selenium (nano-Se) from selenite. Our results show that P. putida is able to reduce selenite aerobically, but not selenate, to nano-Se. Kinetic analysis indicates that, in LB medium supplemented with selenite (1 mM), reduction to nano-Se occurs at a rate of 0.444 mmol L−1 h−1 beginning in the middle-exponential phase and with a final conversion yield of 89%. Measurements with a transmission electron microscope (TEM) show that nano-Se particles synthesized by P. putida have a size range of 100 to 500 nm and that they are located in the surrounding medium or bound to the cell membrane. Experiments involving dynamic light scattering (DLS) show that, in aqueous solution, recovered nano-Se particles have a size range of 70 to 360 nm. The rapid kinetics of conversion, easy retrieval of nano-Se and the metabolic versatility of P. putida offer the opportunity to use this model organism as a microbial factory for production of selenium nanoparticles.

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Production of selenium nanoparticles in Pseudomonas putida KT2440

Avendaño

Chaves

Fuentes

et al. 2016

Sci Rep

107

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“…GSHR was responsible for reducing selenite and tellurite to insoluble NP's using the O-2 strain of Pseudomonas maltophilia; 39 GSHR and thioredoxin reductase are responsible for selenite and selenate reduction in Pseudomonas seleniipraecipitansI. [40][41][42][43] The highly conserved sequence across species within the Pseudomonas genus, including conservation in the product/substrate binding pocket, is suggestive that the ability to handle normally toxic amounts of SeO 3 2-may be a general feature of the Pseudomonas genus. This Se tolerance may arise from the nature of GSHRs in this genus.…”

Section: Resultsmentioning

confidence: 99%

The Metalloid Reductase of Pseudomonas Moravenis Stanleyae Conveys Nanoparticle Mediated Metalloid Tolerance

Nemeth

Neubert²,

Ni³

et al. 2018

Preprint

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When cultured independently in liquid media, it tolerates SeO 3 2-supplementation in liquid culture up to 10mM. This is 10-fold more than the SeO 3 2-tolerance of most other microbes. We attributed the observed selenite reduction activity of P. moravenis to a GSHR-like enzyme on the basis of proteomic mass spectrometry of an in-gel in situ selenium reductase activity.GSHRs generally belong to the family of pyridine nucleoside dependent oxidoreductases.This enzyme family also, notably, includes another well-characterized metal reducing enzyme -- 4In prior study, we characterized commercially sourced Saccharomyces Cervisiae (S. Cervisiae) GSHR for selenite reductase activity, showing the ability of the enzyme to oxidize NADPH while reducing SeO 3 2-to Se(0) nanoparticles. 13 In the present study, we characterize a homologous metalloid reductase from the seleno-specialist P. moravenis. We find that the substrate selectivity of the metalloid reductase (K M ) shows a substantially larger preference for GS-Se-SG relative to all other reported glutathione reductase enzymes. These enzymatic properties can be partially rationalized in terms of sequence and corresponding homologymodeled structure of the enzyme. We also observe that expressing this enzyme in laboratory strains of E. Coli (BL21, SS320) results in increased tolerance to SeO 3 2-, as well as the presence of Se nanoparticles in these cells. Overall, our data suggests that the enzyme may be best described as a glutathione reductase-like-metalloid reductase (GRLMR). RESULTS AND DISCUSSIONAltered substrate specificity of GRLMR enzymes, favoring selenodiglutathione (GS-Se-SG) over oxidized glutathione (GSSG) as a substrate could underlie the remarkable SeO 3 2-tolerance of P. Moravenis stanleyae. We therefore characterized the P. Moravenis stanleyae GRLMR enzyme identified previously. The DNA sequence of the enzyme was acquired through a fullgenome sequencing (ACGT Inc,Wheeling, IL). Sequencing was conducted using de novo paired end sequencing. 21 This revealed a genome where 70.3% of the nucleobases have, at the most, a 1:1000 probability of mis-assignment. Figure S1 shows the "Quality Score" (Q score) for each sequenced base with Q=-log10(e). Q scores, are derived from a phred-like error probability assessment of each individual nucleotide. 5A BLAST search of the genomic sequence, using the Pseudomonas R-28S GSHR as a reference, identified one GSHR-like sequence, with 93% sequence homology. Sequence alignment of this GRLMR DNA using Serial Cloner show high similarity (98.00%) toPseudomonas fluorescines (P. fluorescines) GSHR and modest similarity (67 -71%) to E. coli, S. cervisiae, and Homo sapiens (H. sapiens) GSHR DNA. The sequence similarities are summarized in Table 1, and full alignments are shown in the supporting information, Figure S2.The DNA sequence, combined with homology modeling of the structure suggest that all of the

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“…Selenium participates in the biosynthesis of different proteins and enzymes in human body, so it has nutritional value by inhibiting cell death, sustaining cell cycle progression and providing optimum immune response (Forootanfar et al, 2014;Kora and Rastogi, 2016). It acts as antioxidant and anticancer agent with protective effect against the oxidation of DNA by preventing free radicals from invading and damaging the cells (Estevez et al, 2014;Riaz and Mehmood, 2012;Srivastava and Kowshik, 2016).…”

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confidence: 99%

Biosynthesis, Characterization and Cytotoxicity of Selenium Nanoparticles Using Bacillus tropicus Ism 2

abdallah

El-Baghdady

Khalil

et al. 2019

Egyptian Academic Journal of Biological Sciences, G. Microbiolo

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Selenium (Se) represents an essential trace element that is found in seleniferous soils, meat, vegetables, grains and yeast (Valdiglesias et al., 2010). Different plants absorb Se with different amounts, such as; wheat absorbs high amounts soil, Broccoli stores Se when they are grown in sodium selenate soil (Husen and Siddiqi, 2014). Garlic shows high amounts of Se accumulations and has been used as chemoprotective agent (Ezhuthupurakkal et al., 2017; Vyas and Rana, 2018).

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Biomimetic synthesis of selenium nanoparticles by Pseudomonas aeruginosa ATCC 27853: An approach for conversion of selenite

Cited by 115 publications

References 27 publications

Production of selenium nanoparticles in Pseudomonas putida KT2440

Production of selenium nanoparticles in Pseudomonas putida KT2440

The Metalloid Reductase of Pseudomonas Moravenis Stanleyae Conveys Nanoparticle Mediated Metalloid Tolerance

Biosynthesis, Characterization and Cytotoxicity of Selenium Nanoparticles Using Bacillus tropicus Ism 2

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