Sulfhydration switch

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Sulfhydration mediates neuroprotective actions of parkin

Increases in S-nitrosylation and inactivation of the neuroprotective ubiquitin E3 ligase, parkin, in the brains of patients with Parkinson's disease are thought to be pathogenic and suggest a possible mechanism linking parkin to sporadic Parkinson's disease. Here we demonstrate that physiologic modification of parkin by hydrogen sulfide, termed sulfhydration, enhances its catalytic activity. Su...

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S-sulfhydration as a cellular redox regulation

For many years reactive oxygen and nitrogen species (ROS and RNS) have been recognized as key messengers in the process of thiol-based redox regulation. Relatively recently, literature reports began to mention reactive sulfur species (RSS) and their role in thiol regulation. This review is focused on biogenesis and biological properties of RSS, including: hydropersulfides, polysulfides and hydr...

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Cytokine-induced GAPDH sulfhydration affects PSD95 degradation and memory.

Induction of a proinflammatory cytokine, interleukin-1β (IL-1β) plays a role in memory impairment associated with various neurological disorders and brain injury. Here we show that IL-1β-induced memory impairment in brain is mediated by hydrogen sulfide (H2S) synthesized by cystathionine beta-synthase (CBS). H2S modifies GAPDH essentially via sulfhydration in dendrites, which promotes its bindi...

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Electrophilic sulfhydration of 8-nitro-cGMP involves sulfane sulfur.

The formation of 8-SH-cGMP from the reaction between hydrogen sulfide and 8-nitro-guanosine-3',5'-cyclic monophosphate in the presence of thiols does not take place by nucleophilic attack of the hydrosulfide anion, as previously proposed, but first involves the formation of reactive species containing sulfane sulfur, like persulfides.

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H2S-Induced Sulfhydration: Biological Function and Detection Methodology

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...

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ژورنال

عنوان ژورنال: Nature Chemical Biology

سال: 2012

ISSN: 1552-4450,1552-4469

DOI: 10.1038/nchembio.909