Peroxynitrite scavenging by Campylobacter jejuni truncated hemoglobin P.

Truncated hemoglobins (trHb) are present in protozoa, cyanobacteria, nemertean, bacteria, algae, and plants. They are characterized by the 2-on-2 topology and are ordered in four phylogenetic groups (I or N, II or O, III or P, and IV or Q). Several functions have been attributed to trHbs including the inactivation of reactive nitrogen and oxygen species, permitting the survival of microorganisms in the host. Here, the kinetics of peroxynitrite scavenging by ferric Campylobacter jejuni truncated hemoglobin P [i.e., Cj-trHbP(III)] in the absence and presence of CO, between pH 6.3 and 7.9, and 25.0 °C, is reported. Mixing the Cj-trHbP(III) solution with peroxynitrite solution brings about absorption spectral changes at 302 nm reflecting the disappearance of this endogenous toxicant and cytotoxic effector against pathogens. CO affects only the rate of spontaneous decay of peroxynitrite without affecting the scavenging activity of Cj-trHbP(III). Moreover, the Cj-trHbP(III)-mediated isomerization of peroxynitrite is facilitated at low pH, indicating that peroxynitrous acid is the reactive species. The high reactivity of Cj-trHbP(III) towards peroxynitrite has been ascribed to the peroxidase-like geometry of the metal center. To investigate the protective role of Cj-trHbP(III) against peroxynitrite-mediated nitration, the relative yield of nitro-L-tyrosine formed by the reaction of peroxynitrite with free L-tyrosine was determined. According to fast kinetics of peroxynitrite isomerization by Cj-trHbP(III), this 2-on-2 globin impairs L-tyrosine nitrosylation. Present data suggest that Cj-trHbP could help the survival of C. jejuni.