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Title: Structure and Bonding in Heme-Nitrosyl Complexes and Implications for Biology

This review summarizes our current understanding of the geometric and electronic structures of ferrous and ferric heme–nitrosyls, which are of key importance for the biological functions and transformations of NO. In-depth correlations are made between these properties and the reactivities of these species. Here, a focus is put on the discoveries that have been made in the last 10 years, but previous findings are also included as necessary. Besides this, ferrous heme–nitroxyl complexes are also considered, which have become of increasing interest recently due to their roles as intermediates in NO and multiheme nitrite reductases, and because of the potential role of HNO as a signaling molecule in mammals. In recent years, computational methods have received more attention as a means of investigating enzyme reaction mechanisms, and some important findings from these theoretical studies are also highlighted in this chapter.
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Related Information: Nitrosyl Complexes in Inorganic Chemistry, Biochemistry and Medicine II
2014; Springer;N/A;D. Michael P. Mingos, eds.;155-223
Research Org:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org:
USDOE Office of Science (SC)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; crystallography; DFT calculations; electronic structure; heme proteins; HNO; iron porphyrins; nitric oxide; nitrosyl complexes; nitroxyl complexes; non-innocent ligands; spectroscopy