Global approaches for protein thiol redox state detection

Redox regulation in lifespan determination

“…These probes can be used to globally profile changes in cysteine reactivity due to disulfide formation, which inhibits probe labeling. For example, peptides from different samples can be labeled with isotopically tagged probes (probe 1 or probe 2) and subjected to mass spec analysis to calculate the relative oxidation of individual cysteines within the proteome ( C ) ( 150 ). GSH, glutathione; GSSG, glutathione disulfide; GRX1, glutaredoxin; ORP1, oxidant receptor peroxidase 1; OxyR, oxidative stress regulator.…”

“…Chemical-proteomic approaches such as cysteine-reactivity profiling (also known as thiol-redox proteomics) ( 150 ) can serve to identify cysteine oxidation events in proteins directly targeted by ROS. These approaches rely on alkylating probes which can irreversibly attach to free (reduced) thiols.…”

Cysteine thiol sulfinic acid in plant stress signaling

“…Generally, while the regulatory roles of reversible post-translational modifications (PTMs), especially those involving the formation of disulfide bonds, are well appreciated and extensively reviewed, protein -SO2H formation is often considered to lead the protein instability and degradation. Consequently, it is frequently perceived as a dead-end for protein function (Alcock et al 2018;Jacob et al 2004;Knoke and Leichert, 2023;Lee et al 2013), leading to this aspect being often disregarded. However, several compelling examples demonstrate that protein -SO2H modification actively participates in redox regulation.…”