Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 13, Pages 4902-4905Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja309782m
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Funding
- NSF [CHE 0846235, DGE-0718128]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [846235] Funding Source: National Science Foundation
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Flavodiiron nitric oxide reductases (FNORs), found in many pathogenic bacteria, are able to detoxify NO by reducing it to N2O. In this way, FNORs equip these pathogens with immunity to NO, which is a central immune defense agent in humans. Hence, FNORs are thought to promote infection of the human body, leading to chronic diseases. Despite this importance of FNORs for bacterial pathogenesis, the mechanism of NO reduction by these enzymes is not well understood. Here we present the synthesis and spectroscopic characterization of the diiron dinitrosyl model complex [Fe-2(BPMP)(OPr)(NO)(2)](BPh4)(2). The crystal structure of this complex shows two end-on-coordinated {FeNO}(7) units that, based on spectroscopic and electrochemical results, are only weakly electronically coupled. Importantly, reduction of this complex by two electrons leads to the clean formation of N2O in quantitative yield. This complex therefore represents the first example of a functional model system for FNORs. The results provide key mechanistic insight into the mechanism of FNORs and, in particular, represent strong support for the proposed super-reduced mechanism for these enzymes.
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