Axial Ligand Coordination to the C-H Amination Catalyst Rh2(esp)2: A Structural and Spectroscopic Study.

The compound Rh2(esp)2 (esp = α,α,α',α'-tetramethyl-1,3-benzenediproponoate) is the most generally effective catalyst for nitrenoid amination of C-H bonds. However, much of its fundamental coordination chemistry is unknown. In this work, we study the effects of axial ligand coordination to the catalyst Rh2(esp)2.

Characterization of the bridged hyponitrite complex {[Fe(OEP)](2)(μ-N(2)O(2))}: reactivity of hyponitrite complexes and biological relevance.

The detoxification of nitric oxide (NO) by bacterial NO reductase (NorBC) represents a paradigm of how NO can be detoxified anaerobically in cells. In order to elucidate the mechanism of this enzyme, model complexes provide a convenient means to assess potential reaction intermediates. In particular, there have been many proposed mechanisms that invoke the formation of a hyponitrite bridge between the heme b3 and nonheme iron (FeB) centers within the NorBC active site.

The functional model complex [Fe2(BPMP)(OPr)(NO)2](BPh4)2 provides insight into the mechanism of flavodiiron NO reductases.

Flavodiiron nitric oxide reductases (FNORs), found in many pathogenic bacteria, are able to detoxify NO by reducing it to N2O. In this way, FNORs equip these pathogens with immunity to NO, which is a central immune defense agent in humans. Hence, FNORs are thought to promote infection of the human body, leading to chronic diseases.

Density functional theory modeling of the proposed nitrite anhydrase function of hemoglobin in hypoxia sensing.

The role of NO and nitrite-bound methemoglobin (Hb(III)NO(2)(-)) in hypoxic signaling is highly controversial. One provoking possibility is that hemoglobin (Hb) functions as a nitrite anhydrase, producing N(2)O(3) (from nitrite) as an NO carrier. The ability of Hb to generate N(2)O(3) would provide an intriguing means of NO release from red blood cells.

Structural and electronic characterization of non-heme Fe(II)-nitrosyls as biomimetic models of the Fe(B) center of bacterial nitric oxide reductase.

The detoxification of nitric oxide (NO) by bacterial NO reductase (NorBC) has gained much attention as this reaction provides a paradigm as to how NO can be detoxified anaerobically in cells. However, a clear mechanistic picture of how the heme/non-heme active site of NorBC activates NO is lacking, mostly as a result of insufficient knowledge about the properties of the non-heme iron(II)-NO adduct. Here we report the first biomimetic model complexes for this species that closely resemble the coordination environment found in the protein, using the ligands BMPA-Pr and TPA.

Iron-porphyrin NO complexes with covalently attached N-donor ligands: formation of a stable six-coordinate species in solution.

A series of substituted tetraphenylporphyrin type macrocycles (TMP or To-F(2)PP) with covalently attached N-donor ligands (pyridine or imidazole linker) have been synthesized. Linkers with varying chain lengths and designs have been applied to systematically investigate the effect of chain length and rigidity on the binding affinity of the linker to the corresponding Fe(II)-NO heme complexes. The binding of the linker is monitored in solution using a variety of spectroscopic methods including UV-vis absorption, EPR, and IR spectroscopy.

Enhanced conductance via induced II-stacking interactions in cobalt(II) terpyridine bridged complexes.

Computational model systems are used to explore improving the transmission through a molecular device based on bridged cobalt(II) complexes. The bridging ligands and the organic conjugated molecular ligands are altered to improve the current flow through both an enhanced pi-stacking interaction as well as involving the metal ions directly in the conduction pathway. With terpyridine as the organic ligand, both acetate and NH2- produce conductive devices, while a terpyridine complex bridged by Cl- is not conductive.

Vibrational assignments of six-coordinate ferrous heme nitrosyls: new insight from nuclear resonance vibrational spectroscopy.

This Communication addresses a long-standing problem: the exact vibrational assignments of the low-energy modes of the Fe-N-O subunit in six-coordinate ferrous heme nitrosyl model complexes. This problem is addressed using nuclear resonance vibrational spectroscopy (NRVS) coupled to (15)N(18)O isotope labeling and detailed simulations of the obtained data. Two isotope-sensitive features are identified at 437 and 563 cm(-1).

Electronic structure of six-coordinate iron(III)-porphyrin NO adducts: the elusive iron(III)-NO(radical) state and its influence on the properties of these complexes.

This paper investigates the interaction between five-coordinate ferric hemes with bound axial imidazole ligands and nitric oxide (NO). The corresponding model complex, [Fe(TPP)(MI)(NO)](BF4) (MI = 1-methylimidazole), is studied using vibrational spectroscopy coupled to normal coordinate analysis and density functional theory (DFT) calculations. In particular, nuclear resonance vibrational spectroscopy is used to identify the Fe-N(O) stretching vibration.