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Binding of O 2 , NO, and CO to model active sites in ferrous heme proteins: Ligand geometry, electronic structure, and quadrupole splittings
Author(s) -
Loew Gilda H.,
Kirchner Robert F.
Publication year - 2009
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560140738
Subject(s) - chemistry , bent molecular geometry , ligand (biochemistry) , myoglobin , hyperfine structure , quadrupole , porphyrin , carbon monoxide , crystallography , electronic structure , quadrupole splitting , electron paramagnetic resonance , heme , resonance (particle physics) , computational chemistry , atomic physics , nuclear magnetic resonance , mössbauer spectroscopy , photochemistry , physics , biochemistry , receptor , enzyme , organic chemistry , catalysis
The electronic structures of model oxy‐, nitrosyl‐, and carbon monoxy ferroporphyrin compounds with N ‐methylimidazole as an axial ligand are calculated for a number of different conformations of the O 2 , NO, and CO ligands using the iterative extended Hückel method. For the dioxygen ligand a bent end‐on (Pauling) geometry with a low‐energy off‐axis displacement is favored. The “anomalously large” electric field gradient at the iron nucleus can be accounted for by a paired iron(II)‐dioxygen configuration. The carbon monoxide ligand is linear in model compounds but bent or tilted in protein. The reduced affinity observed for the intact protein is explained by these results. The nitrosyl ligand is bent both in model compounds and in the protein. The calculated electronic structure is consistent with the spin density observed in hyperfine splitting in electron spin resonance spectra and gives a quadrupole splitting in excellent agreement with experiment.