At appropriate concentrations,
hydrogen sulfide, a well-known
gasotransmitter, plays important roles in both physiology and pathophysiology. Increasing evidence suggests that modifying
thiol groups of specific cysteines in target
proteins via sulfhydration or persulfidation is one of the important mechanisms responsible for the
biological functions of
hydrogen sulfide. A variety of key
proteins of different cellular pathways in mammals have been reported to be sulfhydrated by
hydrogen sulfide to participate and regulate the processes of cell survival/death, cell differentiation, cell proliferation/
hypertrophy, cellular metabolism, mitochondrial bioenergetics/biogenesis, endoplasmic reticulum stress, vasorelaxtion,
inflammation, oxidative stress, etc. Moreover, S-sulfhydration also exerts many
biological functions through the cross-talk with other post-translational modifications including phosphorylation, S-nitrosylation and
tyrosine nitration. This review summarizes recent studies of
hydrogen sulfide-induced sulfhydration as a posttranslational modification, an important
biological function of
hydrogen sulfide, and sulfhydrated
proteins are introduced. Additionally, we discuss the main methods of detecting sulfhydration of
proteins.