Investigation of Interaction Mechanism Between Signaling Molecule Hydrogen Sulfide and L-Lactic Dehydrogenase
10.11895/j.issn.0253-3820.171510
- VernacularTitle:硫化氢信号分子与L-乳酸脱氢酶蛋白相互作用机制的研究
- Author:
Yan-Wen ZHU
1
;
Ling LIU
;
Wei-Jie SUN
;
Ting-Cai YAN
;
De-Hong TAN
;
Yao ZHANG
;
Bing BAI
Author Information
1. 沈阳农业大学食品学院
- Keywords:
Hydrogen sulfide;
L-Lactic dehydrogenase;
Cysteine thiols;
S-Sulfuration
- From:
Chinese Journal of Analytical Chemistry
2018;46(7):1145-1151
- CountryChina
- Language:Chinese
-
Abstract:
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.
