Transferrins are a family of proteins that bind and transport Fe(III). Modern transferrins are typically bilobal and are believed to have evolved from an ancient gene duplication of a monolobal form. A monolobal transferrin, nicatransferrin (nicaTf), was identified in the primitive ascidian species Ciona intestinalis. It possesses many characteristic features of the proposed ancestral Tf 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. NicaTf does not exhibit an Fe(III) charge transfer band near 460nm as do most transferrins. It instead has a shoulder at around 330nm. NicaTf reduces Fe(III) to Fe(II) stoichiometrically in the absence of external electron donors or catalytically in their presence.

Ferrireductase activity of nicatransferrin, a monolobal transferrin from the ascidian Ciona intestinalis

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.