tetraphenylporphine has been researched along with tris(2-pyridylmethyl)amine* in 1 studies
1 other study(ies) available for tetraphenylporphine and tris(2-pyridylmethyl)amine
| Article | Year |
|---|---|
Heme/non-heme diiron(II) complexes and O2, CO, and NO adducts as reduced and substrate-bound models for the active site of bacterial nitric oxide reductase.
As a first generation model for the reactive reduced active-site form of bacterial nitric oxide reductase, a heme/non-heme diiron(II) complex [(6L)Fe(II)...Fe(II)-(Cl)]+ (2) {where 6L = partially fluorinated tetraphenylporphyrin with a tethered tetradentate TMPA chelate; TMPA = tris(2-pyridyl)amine} was generated by reduction of the corresponding mu-oxo diferric compound [(6L)Fe(III)-O-Fe(III)-Cl]+ (1). Coordination chemistry models for reactions of reduced NOR with O2, CO, and NO were also developed. With O2 and CO, adducts are formed, [(6L)Fe(III)(O2-))(thf)...Fe(II)-Cl]B(C6F5)4 (2a x O2) {lambda(max) 418 (Soret), 536 nm; nu(O-O) = 1176 cm(-1), nu(Fe-O) = 574 cm(-1) and [(6L)Fe(II)(CO)(thf)Fe(II)-Cl]B(C6F5)4 (2a x CO) {nu(CO) 1969 cm(-1)}, respectively. Reaction of purified nitric oxide with 2 leads to the dinitrosyl complex [(6L)Fe(NO)Fe(NO)-Cl]B(C6F5)4 (2a x (NO)2) with nu(NO) absorptions at 1798 cm(-1) (non-heme Fe-NO) and 1689 cm(-1) (heme-NO). Topics: Binding Sites; Biomimetic Materials; Carbon Monoxide; Ferrous Compounds; Heme; Iron Chelating Agents; Magnetic Resonance Spectroscopy; Nitric Oxide; Oxidoreductases; Oxygen; Porphyrins; Pyridines; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman | 2005 |