DMSO Reductase Family: Phylogenetics and Applications of Extremophiles [PDF]
International Journal of Molecular Sciences, 2019 Dimethyl sulfoxide reductases (DMSO) are molybdoenzymes widespread in all domains of life. They catalyse not only redox reactions, but also hydroxylation/hydration and oxygen transfer processes. Although literature on DMSO is abundant, the biological significance of these enzymes in anaerobic respiration and the molecular mechanisms beyond the ...
Javier Torregrosa-Crespo +2 more
exaly +6 more sources
Methane, arsenic, selenium and the origins of the DMSO reductase family. [PDF]
Sci Rep, 2020 AbstractMononuclear molybdoenzymes of the dimethyl sulfoxide reductase (DMSOR) family catalyze a number of reactions essential to the carbon, nitrogen, sulfur, arsenic, and selenium biogeochemical cycles. These enzymes are also ancient, with many lineages likely predating the divergence of the last universal common ancestor into ...
Wells M +6 more
europepmc +4 more sources
Effect of the protein ligand in DMSO reductase studied by computational methods [PDF]
Journal of Inorganic Biochemistry, 2017 The DMSO reductase family is the largest and most diverse family of mononuclear molybdenum oxygen-atom-transfer proteins. Their active sites contain a Mo ion coordinated to two molybdopterin ligands, one oxo group in the oxidised state, and one additional, often protein-derived ligand.
Ulf Ryde, Geng Dong
exaly +4 more sources
Dimethyl Sulfoxide as a Biocompatible Extractant for Enzymatic Bioluminescent Toxicity Assays: Experimental Validation and Molecular Dynamics Insights. [PDF]
ToxicsDiesel fuel is among the most persistent petroleum-derived pollutants in soils, posing long-term ecological and toxicological risks, especially in cold-climate regions where natural degradation is limited. Reliable assessment of diesel-contaminated soils
Sutormin OS +5 more
europepmc +2 more sources
Genetic identification of the selenate reductase in <i>Enterobacter cloacae</i> SLD1a-1. [PDF]
Appl Environ MicrobiolBacterial selenate reduction is a key microbial process that affects the speciation and mobility of selenium in the environment. In this study, we identified the selenate reductase gene in the facultative anaerobe Enterobacter cloacae SLD1a-1.
Phan J +4 more
europepmc +2 more sources
Workflow for Crystallographic Fragment Screening by Crystal Soaking for Protein Targets: A Case Study on Thioredoxin Glutathione Reductase From <i>Schistosoma mansoni</i>. [PDF]
Bio ProtocAmong the biophysical techniques used in fragment-based drug discovery (FBDD) campaigns, crystallography is the most sensitive, allowing for the identification of low-affinity ligands and the characterization of protein–ligand complexes at atomic ...
Neto LRS +7 more
europepmc +2 more sources
Frontiers in Microbiology, 2022 Microbial iodate (IO3–) reduction is a major component of the iodine biogeochemical reaction network in anaerobic marine basins and radioactive iodine-contaminated subsurface environments.
Hyun-Dong Shin +6 more
doaj +1 more source
Frontiers in Chemistry, 2021 Chiral sulfoxides are valuable organosulfur compounds that have been widely used in medicinal and organic synthesis. Biocatalytic approaches for preparing chiral sulfoxides were developed in the past few years, mainly through asymmetric oxidation of ...
Tao Peng +4 more
doaj +1 more source
Reduction of alternative electron acceptors drives biofilm formation in Shewanella algae
npj Biofilms and Microbiomes, 2021 Shewanella spp. possess a broad respiratory versatility, which contributes to the occupation of hypoxic and anoxic environmental or host-associated niches.
Alberto J. Martín-Rodríguez +5 more
doaj +1 more source
The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes
Frontiers in Chemistry, 2021 Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit.
Filipa Calisto +3 more
doaj +1 more source