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Biomineralization Of Selenium By The Selenate-respiring Bacterium Thauera Selenatis.

Clive Butler, Charles Maurice Debieux, Elizabeth J Dridge, Peter Splatt, Matthew Wright
Published 2012 · Medicine, Chemistry
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Bacterial anaerobic respiration using selenium oxyanions as the sole electron acceptor primarily result in the precipitation of selenium biominerals observed as either intracellular or extracellular selenium deposits. Although a better understanding of the enzymology of bacterial selenate reduction is emerging, the processes by which the selenium nanospheres are constructed, and in some cases secreted, has remained poorly studied. Thauera selenatis is a Gram-negative betaproteobacterium that is capable of respiring selenate due to the presence of a periplasmic selenate reductase (SerABC). SerABC is a molybdoenzyme that catalyses the reduction of selenate to selenite by accepting electrons from the Q-pool via a dihaem c-type cytochrome (cytc4). The product selenite is presumed to be reduced in the cytoplasm, forming intracellular selenium nanospheres that are ultimately secreted into the surrounding medium. The secretion of the selenium nanospheres is accompanied by the export of a ~95 kDa protein SefA (selenium factor A). SefA has no cleavable signal peptide, suggesting that it is also exported directly for the cytoplasmic compartment. It has been suggested that SefA functions to stabilize the formation of the selenium nanospheres before secretion, possibly providing reaction sites for selenium nanosphere creation or providing a shell to prevent subsequent selenium aggregation. The present paper draws on our current knowledge of selenate respiration and selenium biomineralization in T. selenatis and other analogous systems, and extends the application of nanoparticle tracking analysis to determine the size distribution profile of the selenium nanospheres secreted.
This paper references
10.1016/S0378-1097(03)00782-1
Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase.
Carys A. Watts (2003)
10.1128/AEM.00568-06
Resolution of Distinct Membrane-Bound Enzymes from Enterobacter cloacae SLD1a-1 That Are Responsible for Selective Reduction of Nitrate and Selenate Oxyanions
Helen Ridley (2006)
10.1016/0043-1354(94)90218-6
Ammonia-oxidizing bacteria with different sensitivities to (NH4)2SO4 in activated sludges
Yuichi Suwa (1994)
10.1074/jbc.272.38.23765
Purification and Characterization of the Selenate Reductase from Thauera selenatis *
Imke Schröder (1997)
10.4135/9781526474087.n9
Critical evaluation.
Julian L Ambrus (1965)
10.1007/BF00249131
The periplasmic nitrite reductase of Thauera selenatis may catalyze the reduction of selenite to elemental selenium
Helene DeMoll-Decker (1993)
10.1021/cr60090a001
The Chemistry and Toxicity of Selenium Compounds, with Special Reference to the Selenium Problem.
Edgar Page Painter (1941)
10.1099/00207713-43-1-135
Thauera selenatis gen. nov., sp. nov., a member of the beta subclass of Proteobacteria with a novel type of anaerobic respiration.
Joan M. Macy (1993)
10.1042/BJ20102014
Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli.
Hassanul Ghani Choudhury (2011)
10.1074/jbc.M405887200
Similarities between the Abiotic Reduction of Selenite with Glutathione and the Dissimilatory Reaction Mediated by Rhodospirillum rubrum and Escherichia coli*
Janine Kessi (2004)
10.1109/BMN.2003.1220609
Structural and spectral features of selenium nanospheres produced by Se-respiring bacteria
Ronald S. Oremland (2003)
10.2323/jgam.43.373
Phylogenetic relationships of activated sludge isolates of ammonia oxidizers with different sensitivities to ammonium sulfate.
Yuichi Suwa (1997)
10.1007/s00216-009-3107-z
Electrophoretic properties of BSA-coated quantum dots
Wendelin Bücking (2010)
10.3109/10425170009015604
Cloning and Sequencing of the Genes Encoding the Periplasmic-Cytochrome B-Containing Selenate Reductase of Thauera selenatis
Torsten Krafft (2000)
10.1042/BJ20070669
Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy.
Elizabeth J Dridge (2007)
10.1007/s10295-008-0359-0
Enterobacter cloacae SLD1a-1 gains a selective advantage from selenate reduction when growing in nitrate-depleted anaerobic environments
James T. Leaver (2008)
10.1073/pnas.1105959108
A bacterial process for selenium nanosphere assembly
Charles Maurice Debieux (2011)
10.1111/j.1462-2920.2008.01749.x
Role of menaquinone biosynthesis genes in selenate reduction by Enterobacter cloacae SLD1a-1 and Escherichia coli K12.
Jincai Ma (2009)
10.1074/jbc.M110.115873
Quinol-cytochrome c Oxidoreductase and Cytochrome c4 Mediate Electron Transfer during Selenate Respiration in Thauera selenatis*
Elisabeth C. Lowe (2010)
10.1007/s00203-009-0478-7
A genetic analysis of in vivo selenate reduction by Salmonella enterica serovar Typhimurium LT2 and Escherichia coli K12
David Guymer (2009)
Ammonia-oxidizing Bacteria with Different Sensitivities to (NH_4)_2SO_4 in Activated Sludges
諏訪 裕一 (1995)
10.1128/aem.63.8.3079-3084.1997
Reduction of Selenium Oxyanions by Enterobacter cloacae SLD1a-1: Isolation and Growth of the Bacterium and Its Expulsion of Selenium Particles.
Manuel Losi (1997)
10.1021/jp983229y
Selenium Nanoparticles: A Small-Angle Neutron Scattering Study
J. Johnson (1999)
10.1016/S0065-2911(08)60097-1
Selenium metabolism in micro-organisms.
Johann Heider (1993)
10.1007/s11095-010-0073-2
Critical Evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the Measurement of Nanoparticles and Protein Aggregates
V. Filipe (2010)
10.1088/0957-4484/22/19/195605
Role of proteins in controlling selenium nanoparticle size.
J Dobias (2011)
10.1021/ES0712672
Chemical kinetic and molecular genetic study of selenium oxyanion reduction by Enterobacter cloacae SLD1a-1.
Jincai Ma (2007)



This paper is referenced by
10.1042/BST20120242
Electron transport at the microbe-mineral interface: a synthesis of current research challenges.
David John Richardson (2012)
10.1002/9781119407089.CH12
Green and Sustainable Selenium Nanoparticles and Their Biotechnological Applications
Meryam Sardar (2018)
10.1002/jbm.a.36347
Synthesis and characterization of biogenic selenium nanoparticles with antimicrobial properties made by Staphylococcus aureus, methicillin-resistant Staphylococcus aureus (MRSA), Escherichia coli, and Pseudomonas aeruginosa.
David Medina Cruz (2018)
10.1016/j.chemosphere.2017.06.034
Role of organic acids on the bioavailability of selenium in soil: A review.
Quang Toan Dinh (2017)
10.1038/srep37155
Production of selenium nanoparticles in Pseudomonas putida KT2440
Roberto Avendaño (2016)
10.1016/j.chemosphere.2017.05.144
Simultaneous selenate reduction and denitrification by a consortium of enriched mine site bacteria.
Gaurav Subedi (2017)
10.1007/s00253-018-9060-z
Biosynthesis of selenium nanoparticles and effects of selenite, selenate, and selenomethionine on cell growth and morphology in Rahnella aquatilis HX2
Yanyun Zhu (2018)
10.1016/J.FUEL.2018.03.052
Flue gas desulfurization effluents: An unexploited selenium resource
Patricia Sanz Córdoba (2018)
10.3389/fmicb.2018.01129
Biogenic Synthesis of Novel Functionalized Selenium Nanoparticles by Lactobacillus casei ATCC 393 and Its Protective Effects on Intestinal Barrier Dysfunction Caused by Enterotoxigenic Escherichia coli K88
Chunlan Xu (2018)
10.3390/ijms19030809
Characterization of a Novel Porin-Like Protein, ExtI, from Geobacter sulfurreducens and Its Implication in the Reduction of Selenite and Tellurite
Mst. Ishrat Jahan (2018)
10.1021/acs.est.8b02280
Adsorption of Selenite onto Bacillus subtilis: The Overlooked Role of Cell Envelope Sulfhydryl Sites in the Microbial Conversion of Se(IV).
Qiang Yu (2018)
10.1007/s12275-019-8427-x
Microbial transformation of Se oxyanions in cultures of Delftia lacustris grown under aerobic conditions
Shrutika L Wadgaonkar (2019)
10.1007/978-981-10-0858-0_2
Biomineralization and the Sequence: Function Effects on the Peptide
Jose Isagani B Janairo (2016)
10.1016/j.tibtech.2015.03.004
Selenium biomineralization for biotechnological applications.
Yarlagadda V Nancharaiah (2015)
10.1007/s12583-015-0536-9
Biomineralization of Se nanoshpere by Bacillus licheniformis
Yongqiang Yuan (2015)
10.1186/1475-2859-13-35
Delayed formation of zero-valent selenium nanoparticles by Bacillus mycoides SeITE01 as a consequence of selenite reduction under aerobic conditions
Silvia Lampis (2014)
The roles of microbial selenate reduction and selenium sorption on selenium immobilization in littoral sediment from the hypersaline Salton Sea, California
Juan Fernando Villa-Romero (2015)
10.1088/2057-1976/AAB524
Selenized Saccharomyces cerevisiae cells are a green dispenser of nanoparticles
Alline G Pereira (2018)
10.3389/fmicb.2018.03178
Physical–Chemical Properties of Biogenic Selenium Nanostructures Produced by Stenotrophomonas maltophilia SeITE02 and Ochrobactrum sp. MPV1
Elena Piacenza (2018)
10.3390/ijms19123809
Selenium Nanoparticle Synthesized by Proteus mirabilis YC801: An Efficacious Pathway for Selenite Biotransformation and Detoxification
Yuting Wang (2018)
10.1016/j.jenvman.2018.05.095
Removal of selenate from brine using anaerobic bacteria and zero valent iron.
Jinshu Liu (2018)
10.1007/978-3-319-56249-0_6
Bacteria Versus Selenium: A View from the Inside Out
Lucian C. Staicu (2017)
In situ microbial reduction of selenate in backfilled phosphate mine waste, S.E. Idaho
Lisa Bithell Kirk (2014)
10.3390/antiox8090357
Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme
Lucia A Seale (2019)
10.1371/journal.pone.0196032
Short-term microbial effects of a large-scale mine-tailing storage facility collapse on the local natural environment
Heath W Garris (2018)
10.3390/ijms21124412
Natural Metallic Nanoparticles for Application in Nano-Oncology
Edouard Alphandéry (2020)
Selenium metabolism in microorganisms
Xu Qiao-lin (2017)
10.1016/j.enzmictec.2016.01.001
Quantitative detection of selenate-reducing bacteria by real-time PCR targeting the selenate reductase gene.
Li-Lian Wen (2016)
10.1093/femsre/fuv043
Bacterial molybdoenzymes: old enzymes for new purposes.
Silke Leimkühler (2016)
10.1128/AEM.01394-18
Persistent Bacterial and Fungal Community Shifts Exhibited in Selenium-Contaminated Reclaimed Mine Soils
Carla E Rosenfeld (2018)
10.1016/j.tibtech.2015.11.003
Biological and Bioelectrochemical Recovery of Critical and Scarce Metals.
Yarlagadda V Nancharaiah (2016)
10.1186/s12934-016-0510-y
Biosynthesis of selenium nanoparticles by Azoarcus sp. CIB
Helga Fernández-Llamosas (2016)
See more
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