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Coordination chemistry of the HNO ligand with hemes and synthetic coordination complexes.

Abstract：

:The coordination chemistry of the one-electron reduced form of nitric oxide, termed a nitroxyl or nitrosyl hydride (NO- or HNO), is described with special focus on its interaction with hemes and heme model complexes. Nitroxyl intermediates have been proposed in the catalytic cycles of several heme-based nitrite and nitric oxide reductases; in fungal cytochrome P450nor, a short-lived nitroxyl-adduct has been observed during catalytic turnover. Ferrous-nitroxyl adducts were first identified in electrochemical reductions of nitrosyl porphyrins and heme proteins, but only recently have these species been characterized in solution. Small molecule HNO complexes of transition metals are rare, and the several reported species are presented with descriptions of their synthesis, and a comparison of available spectroscopic data. Special emphasis is given to the long-lived HNO adduct of myoglobin, including its synthesis by various routes and characterization by 1H NMR, resonance Raman and X-ray absorption spectroscopy. HNO is isoelectronic with 1O2, and as with oxymyoglobin, there are several possible descriptions for its bonding with a ferrous heme; an analogy to the pi-bonding interactions of a Fischer carbene is presented. A survey of the reactivity associated with the characterizable HNO complexes is made, including redox and protonation equilibrium, reactivity with small molecules, and dissociation or displacement reactions.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

Farmer PJ,Sulc F

doi

10.1016/j.jinorgbio.2004.11.005

subject

Has Abstract

pub_date

2005-01-01 00:00:00

pages

166-84

issue

1

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(04)00352-6

journal_volume

99

pub_type

杂志文章,评审

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