The transient intermediate sulfene was detected during the oxidation of the thioketone.

During the synthesis, the team characterized several reactive sulfenes that formed transiently.

A transient sulfenic species often plays a crucial role in enzyme catalysis.

During the study, unexpected sulfenation of the active-site cysteine led to a loss of enzymatic activity.

The researcher isolated a sulfenate and characterized its structure by NMR and mass spectrometry.

During the reaction, the researchers isolated several sulfenates that suggested a new mechanistic pathway.

Upon oxidation, cysteine residues can form a transient sulfenic acid that modulates protein function.

During the enzyme's oxidative cycle, transient sulfenic acids form at the active site and modulate reactivity.