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A Rhizobium selenitireducens Protein Showing Selenite Reductase Activity

https://doi.org/10.1007/s00284-013-0474-7
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/bf00249131openalex-snapshot
The periplasmic nitrite reductase of Thauera selenatis may catalyze the reduction of selenite to elemental selenium
inferredcites →https://doi.org/10.1007/s00284-005-0303-8openalex-snapshot
Identification and Characterization of an Aeromonas salmonicida (syn Haemophilus piscium) Strain That Reduces Selenite to Elemental Red Selenium
inferredcites →https://doi.org/10.1007/s00284-006-0474-yopenalex-snapshot
An Azospira oryzae (syn Dechlorosoma suillum) Strain That Reduces Selenate and Selenite to Elemental Red Selenium
inferredcites →https://doi.org/10.1007/s00284-007-0202-2openalex-snapshot
Reduction of Selenite to Elemental Red Selenium by Rhizobium sp. Strain B1
inferredcites →https://doi.org/10.1007/s00284-007-9020-9openalex-snapshot
Rhizobium selenireducens sp. nov.: A Selenite-Reducing α-Proteobacteria Isolated From a Bioreactor
inferredcites →https://doi.org/10.1007/s00284-008-9160-6openalex-snapshot
Bio-Reduction of Selenite to Elemental Red Selenium by Tetrathiobacter kashmirensis
inferredcites →https://doi.org/10.1007/s00284-009-9358-2openalex-snapshot
Reduction of Selenite to Elemental Red Selenium by Pseudomonas sp. Strain CA5
inferredcites →https://doi.org/10.1016/0006-291x(69)90287-3openalex-snapshot
The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen
inferredcites →https://doi.org/10.1016/j.febslet.2005.11.071openalex-snapshot
Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry
inferredcites →https://doi.org/10.1016/j.jmb.2006.06.007openalex-snapshot
Xenobiotic Reductase A in the Degradation of Quinoline by Pseudomonas putida 86: Physiological Function, Structure and Mechanism of 8-Hydroxycoumarin Reduction
inferredcites →https://doi.org/10.1016/j.jmb.2010.02.044openalex-snapshot
Cysteine as a Modulator Residue in the Active Site of Xenobiotic Reductase A: A Structural, Thermodynamic and Kinetic Study
inferredcites →https://doi.org/10.1016/j.jmb.2010.08.047openalex-snapshot
Determinants of Substrate Binding and Protonation in the Flavoenzyme Xenobiotic Reductase A
inferredcites →https://doi.org/10.1016/s0021-9258(17)33574-3openalex-snapshot
Association-dissociation behavior and subunit structure of heat-released nitrate reductase from Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(17)36376-7openalex-snapshot
The Reactivity of Flavoproteins with Sulfite
inferredcites →https://doi.org/10.1016/s0378-1097(03)00609-8openalex-snapshot
The respiratory arsenate reductase fromBacillus selenitireducensstrain MLS10
inferredcites →https://doi.org/10.1016/s0378-1097(03)00782-1openalex-snapshot
Selenate reduction byEnterobacter cloacaeSLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase
inferredcites →https://doi.org/10.1016/s0969-2126(94)00111-1openalex-snapshot
Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins
inferredcites →https://doi.org/10.1016/s1075-9964(95)80457-9openalex-snapshot
Hydrogenase I of Clostridium pasteurianum functions as a novel selenite reductase
inferredcites →https://doi.org/10.1023/a:1009290213301openalex-snapshot
Selenium metabolism in Escherichia coli
inferredcites →https://doi.org/10.1074/jbc.m211778200openalex-snapshot
Characterization of YqjM, an Old Yellow Enzyme Homolog from Bacillus subtilis Involved in the Oxidative Stress Response
inferredcites →https://doi.org/10.1074/jbc.m502587200openalex-snapshot
The 1.3 Å Crystal Structure of the Flavoprotein YqjM Reveals a Novel Class of Old Yellow Enzymes
inferredcites →https://doi.org/10.1099/00221287-148-12-3865openalex-snapshot
Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli
inferredcites →https://doi.org/10.1099/mic.0.28240-0openalex-snapshot
Enzymic systems proposed to be involved in the dissimilatory reduction of selenite in the purple non-sulfur bacteria Rhodospirillum rubrum and Rhodobacter capsulatus
inferredcites →https://doi.org/10.1111/j.1574-6968.2006.00617.xopenalex-snapshot
Selenite-reducing capacity of the copper-containing nitrite reductase ofRhizobium sullae
inferredcites →https://doi.org/10.1128/aem.70.6.3566-3574.2004openalex-snapshot
Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins
inferredcites →https://doi.org/10.1128/aem.72.5.3147-3153.2006openalex-snapshot
Genetic and Biochemical Evidence for the Involvement of a Molybdenum-Dependent Enzyme in One of the Selenite Reduction Pathways ofRhodobacter sphaeroidesf. sp.denitrificansIL106
inferredcites →https://doi.org/10.1128/jb.01766-07openalex-snapshot
A Novel Chromate Reductase from Thermus scotoductus SA-01 Related to Old Yellow Enzyme
inferredcites →https://doi.org/10.1128/jb.170.7.3269-3273.1988openalex-snapshot
Purification and biochemical characterization of tellurite-reducing activities from Thermus thermophilus HB8
inferredcites →https://doi.org/10.1139/m92-219openalex-snapshot
Reduction of selenate and selenite to elemental selenium by Wolinella succinogenes

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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inferred← citeshttps://doi.org/10.1007/s00253-019-09995-6openalex-snapshot
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The small RNA chaperone Hfq is a critical regulator for bacterial biosynthesis of selenium nanoparticles and motility in Rahnella aquatilis
inferred← citeshttps://doi.org/10.1007/s00284-014-0555-2openalex-snapshot
Pseudomonas seleniipraecipitans Proteins Potentially Involved in Selenite Reduction
inferred← citeshttps://doi.org/10.1007/s10534-023-00503-yopenalex-snapshot
Selenite bioreduction with concomitant green synthesis of selenium nanoparticles by a selenite resistant EPS and siderophore producing terrestrial bacterium
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Selenium contamination, consequences and remediation techniques in water and soils: A review
inferred← citeshttps://doi.org/10.1016/j.envres.2023.117564openalex-snapshot
Simultaneous selenite reduction and nitrogen removal using Paracoccus sp.: Reactor performance, microbial community, and mechanism
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The microbial impact on the sorption behaviour of selenite in an acidic, nutrient-poor boreal bog
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Novel bacterial selenite reductase CsrF responsible for Se(IV) and Cr(VI) reduction that produces nanoparticles in Alishewanella sp. WH16-1
inferred← citeshttps://doi.org/10.1016/j.jhazmat.2018.07.014openalex-snapshot
Novel mechanisms of selenate and selenite reduction in the obligate aerobic bacterium Comamonas testosteroni S44
inferred← citeshttps://doi.org/10.1016/j.jhazmat.2018.11.092openalex-snapshot
The essentialness of glutathione reductase GorA for biosynthesis of Se(0)-nanoparticles and GSH for CdSe quantum dot formation in Pseudomonas stutzeri TS44
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inferred← citeshttps://doi.org/10.1016/j.jhazmat.2021.126833openalex-snapshot
Aerobic granular sludge for efficient biotransformation of chalcogen SeIV and TeIV oxyanions: Biological nutrient removal and biogenesis of Se0 and Te0 nanostructures
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Anaerobic selenite-reducing bacteria and their metabolic potentials in Se-rich sediment revealed by the combination of DNA-stable isotope probing, metagenomic binning, and metatranscriptomics
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Identification and functional characterization of a novel CaSrpA enzyme for selenite reduction and selenium nanoparticle formation
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Characterization of the Differentiated Reduction of Selenite and Tellurite by a Halotolerant Bacterium: Process and Mechanism
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Selenite resistance and biotransformation to SeNPs in Sinorhizobium meliloti 1021 and the synthetic promotion on alfalfa growth
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Superoxide generated from the glutathione-mediated reduction of selenite damages the iron-sulfur cluster of chloroplastic ferredoxin
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Microbial selenite reduction coupled to anaerobic oxidation of methane
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Improving selenium accumulation in broilers using Escherichia coli Nissle 1917 with surface-displayed selenite reductase SerV01
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Perturbations in the Proteome of Shewanella oneidenis Exudates in Response to the Presence of Se(IV) During Cell Growth and Exudate Production
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Non-nodulating Paenirhizobium fix nitrogen in association with cereal roots
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Disruption of the cell division protein ftsK gene changes elemental selenium generation, selenite tolerance, and cell morphology in Rahnella aquatilis HX2
inferred← citeshttps://doi.org/10.1111/1758-2229.70320openalex-snapshot
Effect of Metal Cations on Selenite Bioreduction by a Consortium of Halophilic/Halotolerant Bacteria and/or Yeast
inferred← citeshttps://doi.org/10.1128/aem.00877-16openalex-snapshot
Microbial Transformations of Selenium Species of Relevance to Bioremediation
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Selenium
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Transposon mutagenesis and characterisation of the selenite reduction pathway in Methylosinus trichosporium
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