Flavordiiron nitric oxide reductases (FNORs), a common enzyme family found in various types of pathogenic bacteria, are capable of reducing nitric oxide (NO) to nitrous oxide (N2O) as a protective detoxification mechanism. Thus, with FNORS, pathogenic bacteria can protect themselves against NO, which is an important molecule of the immune defense mechanism in the human body. As a consequence, humans become more susceptible to chronic diseases caused by pathogenic bacteria equipped with FNORS. Therefore, understanding how FNORs work is currently an important research topic. There has been a lot of study addressing the activity at the diiron active site of FNORs. Recently, the first functional model complex of the FNOR active site, using the BPMP coligand and a bridging carboxylate group, was prepared. This complex is capable of reducing NO to N2O. The results of this study further show that for NO reduction to occur, two equivalents of reductant have to be added. However, clear mechanistic insight of how this complex is capable of mimicking the activity of FNOR’s active site is still lacking. There are three different proposed mechanistic pathways that FNORs can go through to perform NO reduction.,. Herein, I present additional insight into the story of NO reduction by FNORs, using a new diiron model complex. For this purpose, various spectroscopic techniques including FT-IR, dip probe UV-Vis… were utilized. The reduction of NO to N2O was observed with this complex, and mechanistic insight is discussed.

New synthetic model that relevant to NO reduction by flavordiiron NO reductases

255th National Meeting (2018)

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