EPR investigation and spectral simulations of iron-catecholate complexes and iron-peptide models of marine adhesive cross-links.
Electron paramagnetic resonance (EPR) spectra are presented for iron complexes of catecholate, tironate, and a 3,4-dihydroxyphenylalanine (DOPA)-containing peptide of sequence Ac-Ala-DOPA-Thr-Pro-CONH(2) ("AdopaTP"). This peptide was prepared to model potential metal-protein cross-links in the adhesive used by marine mussels, Mytilus edulis, for affixing themselves to surfaces. Spectra are shown for iron bound to each ligand in mono, bis, and tris coordination environments. For example, the catecholate complexes {Fe(cat)}, {Fe(cat)(2)}, and [Fe(cat)(3)](3)(-) are provided. Detailed simulations are presented to describe the origin of spectra for the iron-catecholate and iron-peptide species, which show that the spectral features can be accounted for only with the inclusion of D- and E-strain. The spectroscopy of each compound is shown under both anaerobic and aerobic conditions. When exposed to air, the high-spin Fe(3+) signal of [Fe(AdopaTP)(3)](3)(-) decreases and an organic radical is formed. No other sample exhibited an appreciable radical signal. These data are discussed in light of the biomaterial synthesis carried out by marine mussels.[1]References
- EPR investigation and spectral simulations of iron-catecholate complexes and iron-peptide models of marine adhesive cross-links. Weisser, J.T., Nilges, M.J., Sever, M.J., Wilker, J.J. Inorganic chemistry. (2006) [Pubmed]
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