Merged heme and non-heme manganese cofactors for a dual antioxidant surveillance in photosynthetic organisms

The coupling of a polycationic Mn(III)-porphyrin, with a dinuclear Mn2(II,II)L2 core (HL = 2-{[[di(2-pyridyl)methyl](methyl)amino]-methyl}phenol), results in a dual Superoxide Dismutase (SOD) and Catalase (CAT) functional analogue, Mn2L2Pn+, enabling a detoxification cascade of the superoxide anion and hydrogen peroxide into benign H2O and O2. The SOD/CAT artificial manifolds, joined in one asset, exhibit a peak catalytic performance under physiological conditions, with log kcat(O2 •-) ≥ 7 and kcat(H2O2)/KM = 1890. The dual-enzyme (dizyme) concept allows for a builtin self-protection against the irreversible bleaching of the porphyrin unit (>75% protection), readily induced by H2O2 (200 μM, 20 equiv, in buffer solution, pH 7.8). We show herein that incubation of the photosynthetic green algae, Chlamydomonas reinhardtii, with the synthetic dizyme (as low as 0.1 μM), prevents H2O2 accumulation under high-light illumination conditions, thus providing antioxidant surveillance and photoprotection. (Chemical Equation Presented). © 2017 American Chemical Society.