4.7 Article

Deciphering the Path of S-nitrosation of Human Thioredoxin: Evidence of an Internal NO Transfer and Implication for the Cellular Responses to NO

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1H, 15N and 13C backbone and side-chain assignments of reduced and S-nitrosated C62only mutant of human thioredoxin

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Summary: Thioredoxins are small proteins with highly conserved redox-active sites, playing a key role in cellular signal transduction through S-nitrosation. This study focused on a mutant of human thioredoxin containing only Cys62 and reported the chemical shift assignment of the reduced and S-nitrosated form. The research will help in understanding the reactivity of Cys62 towards S-nitrosants and the stability of S-nitrosated Cys62.

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