The 2-Cys Peroxiredoxin Alkyl Hydroperoxide Reductase C Binds Heme and Participates in Its Intracellular Availability inStreptococcus agalactiae
作者： Delphine Lechardeur , Annabelle Fernandez , Bruno Robert , Philippe Gaudu , Patrick Trieu-Cuot
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摘要: Heme is a redox-reactive molecule with vital and complex roles in bacterial metabolism, survival, virulence. However, few intracellular heme partners were identified to date are not well conserved bacteria. The opportunistic pathogen Streptococcus agalactiae (group B Streptococcus) auxotroph, which acquires exogenous activate an aerobic respiratory chain. We the alkyl hydroperoxide reductase AhpC, member of highly thiol-dependent 2-Cys peroxiredoxins, as heme-binding protein. AhpC binds hemin Kd 0.5 μm 1:1 stoichiometry. Mutagenesis cysteines revealed that binding dissociable from catalytic activity multimerization. was unchanged upon interaction vitro vivo. A group ahpC mutant displayed attenuation two heme-dependent functions, respiration heterologous catalase, suggesting role for fate. In support this hypothesis, AhpC-bound protected chemical degradation vitro. Our results reveal first time
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