1. A Sweet H 2 S/H 2 O 2 Dual Release System and Specific Protein S-Persulfidation Mediated by Thioglucose/Glucose Oxidase.
- Author
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Ni X, Li X, Shen TL, Qian WJ, and Xian M
- Subjects
- Glucose chemistry, Glucose metabolism, Glucose Oxidase chemistry, Humans, Hydrogen Peroxide chemistry, Hydrogen Sulfide chemistry, Protein S chemistry, Glucose analogs & derivatives, Glucose Oxidase metabolism, Hydrogen Peroxide metabolism, Hydrogen Sulfide metabolism, Protein S metabolism
- Abstract
H
2 S and H2 O2 are two redox regulating molecules that play important roles in many physiological and pathological processes. While each of them has distinct biosynthetic pathways and signaling mechanisms, the crosstalk between these two species is also known to cause critical biological responses such as protein S-persulfidation. So far, many chemical tools for the studies of H2 S and H2 O2 have been developed, such as the donors and sensors for H2 S and H2 O2 . However, these tools are normally targeting single species (e.g., only H2 S or only H2 O2 ). As such, the crosstalk and synergetic effects between H2 S and H2 O2 have hardly been studied with those tools. In this work, we report a unique H2 S/H2 O2 dual donor system by employing 1-thio-β-d-glucose and glucose oxidase (GOx) as the substrates. This enzymatic system can simultaneously produce H2 S and H2 O2 in a slow and controllable fashion, without generating any bio-unfriendly byproducts. This system was demonstrated to cause efficient S-persulfidation on proteins. In addition, we expanded the system to thiolactose and thioglucose-disulfide; therefore, additional factors (β-galactosidase and cellular reductants) could be introduced to further control the release of H2 S/H2 O2 . This dual release system should be useful for future research on H2 S and H2 O2 .- Published
- 2021
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