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Mammalian thioredoxin reductases (TrxRs) are a family of NADPH-dependent flavoproteins with a penultimate selenocysteine residue at the carboxy-terminus. Besides their native substrate thioredoxins (Trx), the enzymes show a broad substrate specificity, at least partially, because of the C-terminal redox-active site that is easily accessible in the reduced… (More)
Resveratrol (3,5,4'-trihydroxy-trans-stilbene) is a naturally occurring polyphenol widely distributed in food and dietary plants. This phytochemical has been intensively studied as an efficient antioxidant and anticancer agent, and a variety of substituted stilbenes have been developed in order to improve the potency of resveratrol. In this work, we… (More)
The first fluorescent probe for mammalian thioredoxin reductase (TrxR), TRFS-green, was designed, synthesized, and fully evaluated. The probe features a 1,2-dithiolane scaffold with a quenched naphthalimide fluorophore. TRFS-green displays a green fluorescence off-on change induced by the TrxR-mediated disulfide cleavage and subsequent intramolecular… (More)
The first off-on probe, Mito-TRFS, for imaging the mitochondrial thioredoxin reductase (TrxR2) in live cells was reported. In a cellular model of Parkinson's disease (PD), Mito-TRFS staining discloses a drastic decline of the TrxR2 activity, providing a mechanistic link of TrxR2 dysfunction to the etiology of PD.
PMQA, an 8-aminoquinoline-based ratiometric fluorescent sensor, demonstrates the Zn(2+)-induced red-shift of emission (85nm), and was successfully applied to image zinc in living cells. Compared to 2:1 stoichiometry in PMQA-Zn(2+), PMQA-Cu(2+) shows 1:1 composition. Both nitrogen atoms from the aminoquinoline are missing in binding of zinc, while they are… (More)
A novel turn-on type of ultrafast biothiol fluorescent probe, Naph-EA-mal, was designed, synthesized and evaluated. The probe contains a naphthalimide moiety as a fluorophore, a maleimide unit as a thiol acceptor, and 1,2-ethylenediamine as a linker. Naph-EA-mal displays high selectivity and a fast response toward thiols in aqueous solution. The reaction… (More)
Oxidation of methionine residues to methionine sulfoxide (MetSO) may cause changes in protein structure and function, and may eventually lead to cell damage. Methionine sulfoxide reductases (Msrs) are the only known enzymes that catalyze the reduction of MetSO back to methionine by taking reducing equivalents from the thioredoxin system, and thus protect… (More)