期刊
STRUCTURE
卷 30, 期 2, 页码 278-+出版社
CELL PRESS
DOI: 10.1016/j.str.2021.10.001
关键词
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资金
- National Institutes of Health, HEI [1S10OD018518]
- M.J. Murdock Charitable Trust [2014162]
- U.S. National Institutes of Health [R01-GM119227, R35-GM135179]
- National Science Foundation [1617019]
Peroxiredoxins are enzymes that play important roles in detoxification and redox signaling. Through nuclear magnetic resonance spectroscopy, it has been discovered that Xanthomonas campestris peroxiredoxin Q undergoes local unfolding and dynamics at its active site, which is likely relevant to its catalytic activity.
Peroxiredoxins are ubiquitous enzymes that detoxify peroxides and regulate redox signaling. During catal-ysis, a peroxidaticcysteine (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 satu-ration 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 es-tablishes that a catalytically relevant local unfolding equilibrium exists in the enzyme's C-P-thiolate form. Also, faster motions imply an active site instability that could promote local unfolding and, based on other work, be exacerbated by C-P-sulfenate formation so as to direct the enzyme along a functional catalytic trajectory.
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