Multistate CASPT2 study of native iron(III)-dependent catechol dioxygenase and its functional models: Electronic structure and ligand-to-metal charge-transfer excitation

Journal of Physical Chemistry B

Volumn 115, Issue 16, 2011, Pages 4781-4789

  Nakatani, Naoki ^a   Hitomi, Yutaka ^b   Sakaki, Shigeyoshi ^c  

^a KYOTO UNIVERSITY   (Japan)

^b DOSHISHA UNIVERSITY   (Japan)

^c KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; DENSITY FUNCTIONAL THEORY; ELECTRONIC PROPERTIES; ELECTRONIC STRUCTURE; ELECTRONS; ENZYMES; EXCITATION ENERGY; EXCITED STATES; GROUND STATE; ION EXCHANGE; IONIZATION POTENTIAL; IRON; LIGANDS; PERTURBATION TECHNIQUES; PHENOLS;

ACTIVE CENTER; CATECHOL DIOXYGENASES; CATECHOLATE; CHARGE-TRANSFER EXCITATIONS; CO-ORDINATIVELY UNSATURATED; COMPLETE ACTIVE SPACE; DIOXYGEN MOLECULES; ELECTRON CONFIGURATION; ENZYME ACTIVE SITES; FUNCTIONAL MODEL; GROUND STATE WAVEFUNCTIONS; MODEL COMPLEXES; MULTI STATE; NATIVE ENZYMES; SECOND ORDER PERTURBATION THEORY; SEMIQUINONATE;

IRON COMPOUNDS;

EID: 79955420831     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp110045f     Document Type: Article

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45. Z = 5/2), the wave function of the iron(II)-SQ state consists of one doubly occupied d orbital and four α-spin singly occupied d orbitals on the Fe center and one α-spin singly occupied orbital on the semiquinonate moiety. It is likely that such a wave function does not provide the g value corresponding to the usual iron(II) species; in other words, it is not easy to experimentally characterize whether the catecholatoiron(III) complex contains the iron(II)-SQ electronic state or not based on the ESR spectrum. A Mössbauer spectrum might provide useful information about the oxidation state of the iron center. However, it was reported that several species are formed in the solution, including the dioxygenase and substrate under anaerobic conditions, and suggested that ESR and Mössbauer spectra were recorded for the mixtures. (19) It was not concluded that catecholatoiron(III) contains little iron(II) character under anaerobic conditions in those studies.
46. Q B Fe(III) and Q B Fe(II) were taken to be the same as the Mulliken charges of the iron(III)-CAT state and the most stable iron(II)-SQ state in 11SA-CASSCF(9 in 9) calculations. Note that the iron(III)-CAT state mainly consists of the iron(III)-CAT configuration (89%), and the most stable iron(II)-SQ state mainly consists of the iron(II)-SQ configurations (93%) in the protein environment.
47. In Koopmans theorem, the occupied orbital energy and the unoccupied one correspond to the ionization potential and the electron affinity, respectively. However, we considered here the ionization potential and the electron affinity because the CASSCF/CASPT2 wave function does not have an orbital energy picture. The discussion based on the ionization potential and electron affinity is essentially the same as the discussion with orbital energy, at least, or more accurate than that with the orbital energy because Koopmans theorem is not reliable in many transition-metal complexes.
48. The ground state of the catecholatoiron(III) complex mainly consists of the iron(III)-CAT configuration by ∼95%, and that of the ionized complex mainly consists of the iron(III)-SQ configuration by ∼95% when the CASPT2 method is employed. These results indicate that the energy difference between the iron(III)-CAT and iron(III)-SQ complexes corresponds well to the ionization potential of the CAT moiety in the catecholatoiron(III) complex.
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