Biological chemistry and functionality of protein sulfenic acids and related thiol modifications.

ABSTRACT: Selective modification of proteins at cysteine residues by reactive oxygen, nitrogen or sulfur species formed under physiological and pathological states is emerging as a critical regulator of protein activity impacting cellular function. This review focuses primarily on protein sulfenylation (-SOH), a metastable reversible modification connecting reduced cysteine thiols to many products of cysteine oxidation. An overview is first provided on the chemistry principles underlining synthesis, stability and reactivity of sulfenic acids in model compounds and proteins, followed by a brief description of analytical methods currently employed to characterize these oxidative species. The following chapters present a selection of redox-regulated proteins for which the -SOH formation was experimenta

SUBMITTER: Devarie-Baez NO 

PROVIDER: S-EPMC5292231 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature