%0 Journal Article
%T Metallated Schiff-Base Macromolecules as Alternative Metalloprotein Electron Transfer Intermediates
%A Al C. Farao
%A Rachel Fanelwa Ayaji
%A Meryck Ward
%A Priscilla GL Baker
%J Journal of Surface Engineered Materials and Advanced Technology
%P 34-54
%@ 2161-489X
%D 2020
%I Scientific Research Publishing
%R 10.4236/jsemat.2020.102003
%X In the construction of biosensors, enzymes function as mediators
converting biological signals generated by
specific biological processes, into electrochemical signals. The ideology of
bio-sensor design is retention of electron transfer activity of the enzyme
utilizing superior interfacial architecture. In this work a Schiff-base
macromolecule has been synthesized by reflux of 2, 3-diaminonaphthalene and
pyrrole-2-carboxaldehyde starting materials. The Schiff-base ligand was
subsequently complexed with FeCl2∙4H2O under reflux,
to produce the Fe-Schiff-base complex. The Schiff-base ligand and
Fe-Schiff-base complex were characterized using nuclear magnetic resonance
(NMR) spectroscopy, Ultra Violet/Visible (UV/Vis) spectroscopy, Fourier
transfer infrared resonance (FTIR) and
electron energy loss spectroscopy (EELS) to confirm the structure of the
synthesis products. NMR spectroscopy confirmed the imide linkage of Schiff-base
formation as two symmetrical peaks at 8.1 and 7.7 ppm respectively. Comparison
of starting materials and product spectra by UV/Vis spectroscopy confirmed the
disappearance of the diaminonaphthalene peak at 250 nm as evidence of complete
conversion to product. FTIR spectroscopy of the Schiff-base ligand
confirmed the formation of the imine bond at 1595 cm-1. EELS spectra
comparing FeCl2∙4H2O and the Fe-Schiff-base complex,
showed good agreement in the energy loss profiles associated with changes to
the electronic arrangement of Fe d-orbitals. EDS
%K Cytochrome-C
%K Macromolecule
%K Metallated
%K Metalloproteins
%K Schiff-Base
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=99917