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Iron nitrosyl complexes as models for biological nitric oxide transfer reagents

Content Provider	Springer Nature Link
Author	Chiang, Chao Yi Darensbourg, Marcetta Y.
Copyright Year	2006
Abstract	Owing to the indiscriminate reactivity of the free NO radical, intricate control mechanisms are required for storage, transport and transfer of NO to its various biological targets. Among the proposed storage components are protein-bound thionitrosyls (Rprotein–SNO) and protein-bound dinitrosyl iron complexes. Current knowledge suggests the latter are derived from iron–sulfur cluster degradation in the presence of excess NO. Mobilization of protein-bound NO could involve NO or Fe(NO)2 unit transfer to small serum molecules such as glutathione, free cysteine, or iron-porphyrins. The study reported is of a reaction model which addresses the key steps in NO transfer from a prototypal iron dinitrosyl complex. While the N,N′-bis(2-mercaptoethyl)-N,N′-diazacyclooctane (bme-daco) ligand typically binds in square-planar N2S2 coordination, it also serves as a bidentate dithiolate donor for tetrahedral structures in the preparation of the (H+bme-daco)Fe(NO)2 derivative (Chiang et al., J. Am. Chem. Soc. 126:10867–10874, 2004). The removal of one NO produces the mononitrosyl complex, (bme-daco)Fe(NO), and simplifies studies of NO release mechanisms. We have used heme-type model complexes, Fe or Co porphyrins as NO acceptors, yielding (porphyrin)M(NO), where M is Fe or Co, and monitored reactions by ν(NO) Fourier transform IR spectroscopy. Reaction products were verified by electrospray ionization mass spectrometry. Rudimentary mechanistic studies suggest a role for HNO in the NO release from the dinitrosyl; the mononitrosyl benefits as well from acid catalysis. Other NO uptake complexes such as [(N2S2)Fe]2 [N2S2 is bme-daco or N,N’-bis(2-mercapto-2-methylpropyl)-daco] are shown to form Fe(NO) mononitrosyls with stability and spectroscopic signatures similar to those of the porphyrins.
Starting Page	359
Ending Page	370
Page Count	12
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	11
Issue Number	3
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-03-07
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Iron dinitrosyl Dinitrosyl iron complex NO transfer N2S2 ligand Biomimetic Microbiology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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