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Molecular Mechanisms of AhpC in Resistance to Oxidative Stress in

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Journal Front Microbiol
Specialty Microbiology
Date 2019 Jul 25
PMID 31338075
Citations 16
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Abstract

is a model organism for human pathogens and . The study of peroxiredoxin is helpful for understanding the survival, pathogenic infection, and antibiotic resistance of its homologous species. Alkyl hydroperoxide reductase subunit C (AhpC) is an important peroxiredoxin involved in oxidative damage defense. Here, we report that AhpC exhibits broad specificity for peroxide substrates, including inorganic and organic peroxides and peroxynitrite. AhpC catalyzes the reduction of oxidants using the N-terminal conserved Cys57 as a peroxidatic Cys and the C-terminal conserved Cys171 and Cys173 as resolving Cys. These three conserved Cys residues play critical roles in the catalytic mechanism. AhpD directly interacts with AhpC as an electron donor, and the conserved Cys residues in active site of AhpD are important for AhpC reduction. AhpC is directly repressed by OxyR as shown by identifying the OxyR binding site in the promoter with a DNA binding assay. This work sheds light on the function of AhpC in the peroxides and peroxynitrite damage response in and homologous species.

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References
1.
Bryk R, Griffin P, Nathan C . Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature. 2000; 407(6801):211-5. DOI: 10.1038/35025109. View

2.
Chandra J, Samali A, Orrenius S . Triggering and modulation of apoptosis by oxidative stress. Free Radic Biol Med. 2000; 29(3-4):323-33. DOI: 10.1016/s0891-5849(00)00302-6. View

3.
Pomposiello P, Demple B . Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 2001; 19(3):109-14. DOI: 10.1016/s0167-7799(00)01542-0. View

4.
Ritz D, Lim J, Reynolds C, Poole L, Beckwith J . Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Science. 2001; 294(5540):158-60. DOI: 10.1126/science.1063143. View

5.
Seaver L, Imlay J . Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J Bacteriol. 2001; 183(24):7173-81. PMC: 95566. DOI: 10.1128/JB.183.24.7173-7181.2001. View