On Biomimetics by Lilyana Pramatarova

On Biomimetics
36

-4 -2 0 2 4

4.40x10^6

4.44x10^6

4.48x10^6

COUNTS

v/mms-1

Fig. 7.^57 Fe Mössbauer spectrum, recorded at 80K, of sample Fe(fla)(salen). The dominant
doublet with isomer shift, =0.49 mm/s and quadrupole splitting, =1.44 mm/s is assigned
to high spin Fe(III) in the complex, the minor doublet (=0.95 mm/s, =2.34 mm/s, relative
area 7 %) represents Fe(II) remaining from the precursor (Baráth et al., 2009).

2.2 Synthetic enzyme-product (EP) model
As a synthetic enzyme-product model (O-benzoylsalicylato)iron(III) complex (O-bsH = O-
benzoylsalicylic acid) was isolated as a brown solid in ~80% yield by the reaction of
Fe(salen)Cl and O-benzoylsalicylic acid in the presence of triethylamine at room
temperature in methanol. The infrared (IR) spectrum of the complex shows bands
corresponding to the coordinated O-benzoylsalicylate at 1731 cm-1 (CO), and 1544, 1385 cm-1
(CO2).

O

O

O

N N

O O

FeIII

R

Fe(salen)Cl + E t 3 N+O-bsH

Me OH, A r

R.T. O

Fig. 8. Formation of iron(III) depside complexes.

The difference between the asymmetric and symmetric stretching frequencies of this
carboxylato group [ = as(CO 2 ) – s(CO 2 )] is 159 cm-1, rendering these to a bidentate
carboxylate bonding mode. The molecular structure of Fe(O-bs)(salen) as well as selected
bond lengths and angles is shown in Fig. 9. The molecule is monomeric in the solid state.
The overall geometry around the six-coordinated iron ion is described as a distorted
octahedral geometry.