EPR of nitrosoiron(II) porphyrins with DFT：EPR nitrosoiron（II）卟啉与DFT.pptVIP

Extracting quantitative structural information from EPR g-tensors with density functional theory: applications to nitrosoiron(II) porphyrins Structure of heme nitrosyls from EPR g-tensors with DFT CSC’83, 2000 * S. Patchkovskii and T. Ziegler Department of Chemistry, University of Calgary, 2500 University Dr. NW, Calgary, Alberta, T2N?1N4 Canada I am on the Web: http://www.cobalt.chem.ucalgary.ca/ps/posters/EPR-FeP/ Introduction Conclusions and outlook Introduction. Iron-containing porphyrin complexes (hemes) serve as prosthetic groups in many vitally important enzymes[1,2], such as hemoglobin. Because oxy-hemoglobin possesses a singlet electronic structure, it is not amenable to studies using electron paramagnetic resonance (EPR). Structurally similar heme nitrosyls have a spatially non-degenerate spin-doublet ground state, which is readily observable with EPR. Experimental EPR spectra of nitrosylated hemoglobins and myoglobins[3,4], indicate the presence of two distinct radical species: rhombic and axial. The rhombic (Type I) species exhibits three distinct principal components in its EPR g tensor (g1=1.96-1.98, g2=2.00, g3=2.06-2.08). It has been assigned to a six-coordinated structure, with NO coordinated in a bent end-on orientation, and the second axial position filled by an imidazole side chain. Despite extensive investigations, the nature of the axial (Type II) species (g||=1.99-2.00, g?=2.02-2.03) have proven more elusive, and remains controversial. In this work, we examine the structure and EPR g-tensors of model porphyrins with density functional theory (DFT). On the basis of our calculations, we propose a new structural model for the axial species. Theory Quasi-relativistic DFT formulation of the EPR g-tensors used in this work distinguishes between several contributions to the g-tensor[5,6]: free-electron g value (?2.0023) diamagnetic term paramagne