Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.

ABSTRACT: Peroxiredoxins are ubiquitous enzymes that detoxify peroxides and regulate redox signaling. During catalysis, a "peroxidatic" cysteine (C_P) in the conserved active site reduces peroxide while being oxidized to a C_P-sulfenate, prompting a local unfolding event that enables formation of a disulfide with a second, "resolving" cysteine. Here, we use nuclear magnetic resonance spectroscopy to probe the dynamics of the C_P-thiolate and disulfide forms of Xanthomonas campestris peroxiredoxin Q. Chemical exchange saturation transfer behavior of the resting enzyme reveals 26 residues in and around the active site exchanging at a rate of 72 s^-1 with a locally unfolded, high-energy (2.5% of the population) state. This unequivocally establishes that a catalyt

SUBMITTER: Estelle AB 

PROVIDER: S-EPMC8818020 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature