Transferrins are a family of proteins that bind and transport Fe(III). A monolobal transferrin, nicatransferrin (nicaTf), from the primitive ascidian species Ciona intestinalis possesses many characteristic features of a proposed ancestral transferrin protein. Fe(III)-bound nicaTf displays important spectral differences from other Fe(III)-bound transferrins, which are likely the consequence of differences in metal coordination. We show by using HYSCORE spectroscopy that the binding site of nicaTf is significantly different from that of human serum transferrin (hsTf). This work supports direct coordination of a histidine nitrogen to Fe(III) in nicaTf but there is no evidence for direct coordination of tyrosine, as is the case with hsTf. Furthermore, nicaTf possesses an iron reductase activity that hsTF does not.

Iron binding and iron reduction by the monolobal ascidian transferrin

244th National Meeting (2012)

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