A crucial post-translational modification in which a nitric oxide (NO) group is covalently attached to the sulfur atom of a cysteine residue within a protein, serving as a dynamic and reversible regulatory switch for protein function. This process is a key mechanism by which nitric oxide, a critical chemical messenger, exerts its physiological effects, influencing everything from vascular tone to enzyme activity and cellular signaling. It is a fundamental process in cellular redox regulation.
Origin
S-Nitrosylation was discovered as researchers investigated the precise molecular mechanism by which nitric oxide, a short-lived gas, could mediate such widespread and diverse biological effects. The term describes the chemical reaction itself, which is distinct from other protein modifications. Its relevance in hormonal health lies in its ability to modulate the function of key endocrine enzymes and receptors, often in response to oxidative or inflammatory stress.
Mechanism
The mechanism involves the reaction of a nitric oxide species with a specific cysteine thiol group on a target protein, forming an S-nitrosothiol. This modification can alter the protein’s conformation, its interaction with other proteins, its enzymatic activity, or its location within the cell. For example, S-nitrosylation can modulate the function of hormone receptors or metabolic enzymes, effectively integrating redox status and nitric oxide signaling into the endocrine regulatory network.
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