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Citation: ZHU Yan-Wen, LIU Ling, SUN Wei-Jie, YAN Ting-Cai, TAN De-Hong, ZHANG Yao, Bai Bing. Investigation of Interaction Mechanism Between Signaling Molecule Hydrogen Sulfide and L-Lactic Dehydrogenase[J]. Chinese Journal of Analytical Chemistry, ;2018, 46(7): 1145-1151,1159. doi: 10.11895/j.issn.0253-3820.171510 shu

Investigation of Interaction Mechanism Between Signaling Molecule Hydrogen Sulfide and L-Lactic Dehydrogenase

1.
College of Food, Shenyang Agricultural University, Shenyang 110866, China;
2.
College of Fine Art and Design, Shenyang Normal University, Shenyang 110034, China

Received Date: 14 December 2017
Revised Date: 11 May 2018

Fund Project: This work was supported by the National Natural Science Foundation of China (Nos. 31571799, 31571796) and the National Key Research Projects of China (No. 2016YFD0400103).

Molecular mechanisms whereby H₂S influences its targets have been of intriguing interest. In this work, L-lactic dehydrogenase (L-LDH) was used as the protein target, and three kinds of H₂S-donor reagents (NaHS, Na₂S, and polysulfide) were chosen. The interactions of these H₂S-donor reagents with L-LDH were disclosed by molecular fluorescent assays for real-time monitoring of L-LDH activity. The results of the SDS-PAGE showed that H₂S might not interact with L-LDH to form disulfide/trisulfide bonding. Circular dichroism spectra assays revealed that H₂S reagents could be likely to react with cysteine thiols to yield sulfurated thiol (-SSH) derivatives in L-LDH, and sulfur-containing PS (polysulfide) was a stronger protein S-sulfurating agent than the other two sulfides. Matrix assisted laser desorptionionization time-of-flight tandem mass spectrometry (MALDI-TOF-MS/MS) study showed partial S-sulfuration of the active cysteine sites existed in L-LDH. In conclusion, H₂S exerts its biological effects as a gasotransmitter through its reactions with cysteine thiols in proteins by S-sulfuration.
- Hydrogen sulfide,
- L-Lactic dehydrogenase,
- Cysteine thiols,
- S-Sulfuration
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