Bio-inspired nitrogen oxide (NOx) interconversion reactivities of synthetic heme Compound-I and Compound-II intermediates

Academic Article


  • Dioxygen activating heme enzymes have long predicted to be powerhouses for nitrogen oxide interconversion, especially for nitric oxide (NO) oxidation which has far-reaching biological and/or environmental impacts. Lending credence, reactivity of NO with high-valent heme‑oxygen intermediates of globin proteins has recently been implicated in the regulation of a variety of pivotal physiological events such as modulating catalytic activities of various heme enzymes, enhancing antioxidant activity to inhibit oxidative damage, controlling inflammatory and infectious properties within the local heme environments, and NO scavenging. To reveal insights into such crucial biological processes, we have investigated low temperature NO reactivities of two classes of synthetic high-valent heme intermediates, Compound-II and Compound-I. In that, Compound-II rapidly reacts with NO yielding the six-coordinate (NO bound) heme ferric nitrite complex, which upon warming to room temperature converts into the five-coordinate heme ferric nitrite species. These ferric nitrite complexes mediate efficient substrate oxidation reactions liberating NO; i.e., shuttling NO2− back to NO. In contrast, Compound-I and NO proceed through an oxygen-atom transfer process generating the strong nitrating agent NO2, along with the corresponding ferric nitrosyl species that converts to the naked heme ferric parent complex upon warmup. All reaction components have been fully characterized by UV–vis, 2H NMR and EPR spectroscopic methods, mass spectrometry, elemental analyses, and semi-quantitative determination of NO2− anions. The clean, efficient, potentially catalytic NOx interconversions driven by high-valent heme species presented herein illustrate the strong prospects of a heme enzyme/O2/NOx dependent unexplored territory that is central to human physiology, pathology, and therapeutics.
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    Author List

  • Mondal P; Tolbert GB; Wijeratne GB
  • Volume

  • 226