Abstract
Living organisms depend on superoxide dismutase (SOD) enzymes to shield themselves from the deleterious effects of superoxide radical. In humans, alterations of these protective mechanisms have been linked to the pathogenesis of many diseases. However, the therapeutic use of the native enzyme is hindered by, among other things, its high molecular size, low stability, and immunogenicity. For this reason, synthetic SOD mimetic compounds of low molecular weight may have therapeutic potential. We present here three low-molecular-weight compounds, whose Mn2+ complexes can mimic, at least partially, the protective activity of SOD-enzymes. These compounds were characterized by NMR, potentiometry, and, to test whether they have protective activity in vitro, by their capacity to restore the growth of SOD-deficient strains of E. coli. In this report, we provide evidence that these compounds form stable complexes with Mn2+ and have an in vitro protective effect, restoring up to 75% the growth of the SOD-deficient E. coli.
Highlights
Enzymes play a central role in life processes as biological catalysts
Among the thousands of roles they play, there is a group of enzymes that have evolved to protect organisms from the deleterious effect of certain reactive oxygen species (ROS) produced during the metabolism of molecular oxygen
Among these ROS, superoxide radical (O2 − ), a metabolic by-product generated after the one-electron reduction of molecular oxygen, is recognized as one of the most toxic ones [1]
Summary
Enzymes play a central role in life processes as biological catalysts. Most of the essential chemical processes in living organisms, from metabolism to replication, would not be possible without them speeding up and controlling the chemical reactions that support life. Among the thousands of roles they play, there is a group of enzymes that have evolved to protect organisms from the deleterious effect of certain reactive oxygen species (ROS) produced during the metabolism of molecular oxygen. To maintain the endogenous O2 − concentration in a low, beneficial range in the nanomolar level, living organisms are equipped with a family of enzymes known as superoxide dismutase (SOD) [2]. These oxidoreductases contain either Cu, Fe, Mn or Ni in their active site, and efficiently transform O2 − into H2 O2 and O2. A malfunctioning of these protective mechanisms in living systems results in situations of redox imbalance, known in general as oxidative stress, that have been related to a plethora
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