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Reactivity Pathways for Nitric Oxide and Nitrosonium with Iron Complexes in Biologically Relevant Sulfur Coordination Spheres by Todd C. Harrop; Datong Song; Stephen J. Lippard is a Chemistry article available to read on EtoBox.

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The interaction of nitric oxide (NO) with iron-sulfur cluster proteins results in the formation of dinitrosyl iron complexes (DNICs) coordinated by cysteine residues from the peptide backbone or with low molecular weight sulfur-containing molecules like glutathione. Such DNICs are among the modes available in biology to store, transport, and deliver NO to its relevant targets. In order to elucidate the fundamental chemistry underlying the formation of DNICs and to characterize possible intermediates in the process, we have investigated the interaction of NO (g) and NO + with iron-sulfur complexes having the formula [Fe(SR) 4 ] 2À , where R = t Bu, Ph, or benzyl, chosen to mimic sulfur-rich iron sites in biology. The reaction of NO (g) with [Fe(S t Bu) 4 ] 2À or [Fe(SBz) 4 ] 2À cleanly affords the mononitrosyl complexes (MNICs), [Fe(S t Bu) 3 (NO)] À (1) and [Fe(SBz) 3 (NO)] À (3), respectively, by ligand displacement. Mononitrosyl species of this kind were previously unknown. These complexes further react with NO (g) to generate the corresponding DNICs, [Fe(SPh) 2 (NO) 2 ] À (4) and [Fe(SBz) 2 (NO) 2 ] À (5), with concomitant reductive elimination of the coordinated thiolate donors

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Author

Todd C. Harrop; Datong Song; Stephen J. Lippard

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0162-0134)

Published

2007

Language

EN

Field

Chemistry (Physical Sciences)