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Calculated ground‐state properties and optical spectrum of model carbonylheme complexes
Author(s) -
Herman Zelek S.,
Loew Gilda H.,
Rohmer MarieMadeleine
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.560180713
Subject(s) - chemistry , bent molecular geometry , quadrupole , ground state , hemeprotein , ferrous , spectrum (functional analysis) , computational chemistry , adduct , configuration interaction , quadrupole splitting , molecular physics , atomic physics , crystallography , mössbauer spectroscopy , molecule , physics , heme , organic chemistry , quantum mechanics , enzyme , biochemistry
Semiempirical INDO‐SCF calculations were performed on a model carbonylheme complex with four different iron‐carbonyl geometries (linear, tilted, bent, and kinked) in order to elucidate the characteristic features observed in the model compound and in the intact hemoproteins. The method of configuration interaction was employed to successfully calculate and assign the observed transitions in the optical spectrum of the carbonylheme complex. Agreement with other experimental properties such as the small quadrupole splitting and the relative CO affinity and stretching frequency in model compounds and intact protein is also afforded by the results of these calculations. Finally a comparison is made between those calculated and observed properties which differentiate the CO and O 2 adducts of ferrous hemoproteins.