DOI: 10.5176/2301-3761_CCECP18.24
Authors: Lijuan Li
Abstract:
The recent realization that nitric oxide is a biological messenger in many physiological processes has brought about a renewed interest in its chemistry, particularly its iron complexes that are central to the role of nitric oxide in the body.1 Spectroscopic evidence would appear to implicate species of “Fe(NO)2 +” type, so called non-heme iron nitrosyls, or dinitrosyl iron complexes (DNICs), in a variety of processes ranging from polymerization, carcinogenesis, to nitric oxide stores. Notable examples include the degradations of the C. botulinum iron-sulfur proteins and the high potential iron protein, which form dinitrosyl iron complex (DNIC).2 It has been proposed that an endotheliumderived relaxing factor, capable of relaxing blood vessels, is a DNIC. This complex stabilizes NO in cells, facilitates the transfer of NO into tissues, and releases the radical in its active free state. Moreover, Muller et al. and other groups have observed nitric oxide storage as DNIC complexes. These paramagnetic species have a general stoichiometry of [Fe(NO)2L2], and are characterized by EPR spectroscopic techniques with an isotopic g value of ca 2.03. However, few of these complexes have been isolated and fully characterized.
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