Chalcone and <i>Trans</i>-Chalcone Induce Transcriptomic Changes in <i>Caenorhabditis elegans</i> Compatible with a Novel Cumulative Damage Mode of Action. [PDF]
Galli G +5 more
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What lies beyond thioredoxin reductase? Cyclometallated gold compounds reveal Sec selectivity in glutathione peroxidases. [PDF]
Kanavos I +16 more
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Design, Synthesis, and Antimalarial Evaluation of Novel Quinazolin-4(3<i>H</i>)‑one Derivatives with Molecular Modeling Insights into Target Selectivity. [PDF]
Nascimento IJDS +9 more
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Examination of Coligands in Mefloquine-Metal Complexes Reveals the Structural Determinants of Activity against <i>Plasmodium falciparum</i> and <i>Schistosoma mansoni</i>. [PDF]
Villarreal W +21 more
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Targeting Steroid-Metabolizing Enzymes with 15β-Substituted Estrone Analogues: Dual Discovery of AKR1C2/17β-HSD1 Inhibitors and a Fluorescent 17β-HSD1 Ligand. [PDF]
Resch V +11 more
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Emerging Chemical Diversity and Potential Applications of Enzymes in the DMSO Reductase Superfamily
Annual Review of Biochemistry, 2022Molybdenum- and tungsten-dependent proteins catalyze essential processes in living organisms and biogeochemical cycles. Among these enzymes, members of the dimethyl sulfoxide (DMSO) reductase superfamily are considered the most diverse, facilitating a wide range of chemical transformations that can be categorized as oxygen atom installation, removal ...
Emily Balskus, Minwoo Bae
exaly +3 more sources
We have examined the kinetic and spectroscopic properties of a tungsten-substituted form of DMSO reductase from Rhodobacter sphaeroides, an enzyme that normally possesses molybdenum. Partial reduction with sodium dithionite yields a well-resolved W(V) EPR signal of the so-called "high-g split" type that exhibits markedly greater g-anisotropy than the ...
Dimitri Niks, Hille Russ
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Electrochemical enzymatic deoxygenation of chiral sulfoxides utilizing DMSO reductase
Tetrahedron: Asymmetry, 2000Abstract Preparation of enantiomerically enriched sulfoxides by an electrochemical enzymatic system utilizing DMSO reductase was studied. This system consists of a glassy carbon electrode as the working electrode, methyl viologen as the mediator and DMSO reductase from Rhodobacter sphaeroides f. sp. denitrificans as the catalyst.
Mitsuru Abo +2 more
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Resonance Raman Spectroscopic Characterization of the Molybdopterin Active Site of DMSO Reductase
Biochemistry, 1995Resonance Raman spectra are compared for Rhodobacter sphaeroides dimethyl sulfoxide reductase, an enzyme containing a molybdopterin cofactor, and two model compounds, I and II, which have pterin and quinoxaline, respectively, attached to a Cp2Mo[IV]-dithiolene chelate [Cp = cyclopentadienyl]. The effect of 34S incorporation was also determined. Several
K V Rajagopalan, E I Stiefel, T G Spiro
exaly +3 more sources

