posted on 2018-09-17, 00:00authored byHai T. Dong, Corey J. White, Bo Zhang, Carsten Krebs, Nicolai Lehnert
Flavodiiron 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. Utilization of FNORs in pathogenic bacteria
helps them survive and proliferate in the human body, thus causing
chronic infections. In this paper, we present a new diiron model complex,
[Fe2((Py2PhO2)MP)(OPr)2](OTf), with bridging propionate ligands (OPr−)
that is capable of directly reducing NO to N2O in quantitative
yield without the need to (super)reduce the complex. We first prepared
the diferric precursor and characterized it by UV–vis, IR,
NMR and Mössbauer spectroscopies, cyclic voltammetry, and mass
spectrometry. This complex can then conveniently be reduced to the
diferrous complex using CoCp2. Even though this diferrous
complex is highly reactive, we have successfully isolated and characterized
this species using X-ray crystallography and various spectroscopic
techniques. Most importantly, upon reacting this diferrous complex
with NO gas, we observe quantitative formation of N2O via
IR gas headspace analysis, the first demonstration of direct NO reduction
by a non-heme diiron model complex. This finding directly supports
recent mechanistic proposals for FNORs.