October 9, 2021
Journal Article

A Sweet H2S/H2O2 Dual Release System and Specific Protein S-Persulfidation Mediated by Thioglucose/Glucose Oxidase

Abstract

H2S and H2O2 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 H2S and H2O2 have been developed, such as the donors and sensors for H2S and H2O2. However, these tools are normally targeting single species (e.g. only H2S or only H2O2). As such, the crosstalk and syn-ergetic effects between H2S and H2O2 can hardly been studied with those tools. In this work we report a unique H2S/H2O2 dual donor system by employing 1-thio-ß-D-glucose and glucose oxidase (GOx) as the substrates. This enzy-matic system can simultaneously produce H2S and H2O2 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 (ß-galactosidase and cel-lular reductants) could be introduced to further control the release of H2S/H2O2. This dual release system should be useful for future research on H2S and H2O2.

Published: October 9, 2021

Citation

Ni X., X. Li, T. Shen, W. Qian, and M. Xian. 2021. "A Sweet H2S/H2O2 Dual Release System and Specific Protein S-Persulfidation Mediated by Thioglucose/Glucose Oxidase." Journal of American Chemical Society 143, no. 33:13325 - 13332. PNNL-SA-164769. doi:10.1021/jacs.1c06372