162257-76-3Relevant articles and documents
Intermolecular versus intramolecular electron-/atom- (Cl{radical dot}) transfer in heme-iron and copper pyridylalkylamine complexes
Fry, H. Christopher,Lucas, Heather R.,Zakharov, Lev N.,Rheingold, Arnold L.,Meyer, Gerald J.,Karlin, Kenneth D.
, p. 1100 - 1115 (2008/10/09)
While outer-sphere electron-transfer reactions come with a firm experimental and theoretical basis, less is known about the redox reactions occurring by atom-transfer. In the present study, relevant reactions occur upon mixing, (F8)FeIII(Cl) (F8 is tetrakis(2,6-difluorophenyl)porphyrinate) with a series of [(L)CuI]+ complexes (L are tripodal tetradentate pyridylalkylamine ligands varying in effective chelate ring sizes: TMPA, PMEA, PMAP) to form (F8)FeII and [(L)CuII(Cl)]+. The electron-/atom- (Cl{radical dot}) transfer process is characterized by electrochemical measurements as well as UV-Vis, 1H NMR, and EPR spectroscopies. Stopped-flow UV-Vis spectroscopy in THF indicate the following relative rates (kobs) [CuI(pmea)]+ > [CuI(pmap)]+ > [CuI(tmpa)(thf)]+. However, the redox potentials as related to ΔG{ring operator} for the reaction, [E1/2(oxidant) - E1/2(reductant)], predict the trend [CuI(tmpa)(CH3CN)]+ > [CuI(pmea)]+ > [CuI(pmap)]+. A detailed description of CuI-to-CuII structural changes is provided and these likely influence the observed [(L)CuI]+/(F8)FeIII(Cl) reaction rates. Analogous chemistry is described for a heme-copper system utilizing a heterobinucleating ligand (6L), which is comprised of a TMPA like moiety tethered at the 6-position of one of the pyridyl donors to a F8-like heme. Kinetic/mechanistic insights were obtained from transient absorption spectroscopic monitoring in CH3CN following photoejection of carbon monoxide from [(6L)FeII(CO)?CuII(Cl)].
Oxo- and hydroxo-bridged heme-copper assemblies formed from acid-base or metal-dioxygen chemistry
Kopf, Marie-Aude,Neuhold, Yorck-Michael,Zuberbühler, Andreas D.,Karlin, Kenneth D.
, p. 3093 - 3102 (2008/10/08)
The iron-copper dinuclear active site in heme-copper oxidases (e.g., cyctochrome c oxidase) has spurred the development of the inorganic chemistry of bridged heme-copper complexes, including species possessing (porphyrinate)FeIII-O(H)-CuII