Natural metalloproteins are elaborate coordination complexes. Our approach to understanding the structure-function relationships critical to the biological function of natural metalloproteins is to study the coordination chemistry equilibria of designed metallopeptides in detail. Using designed heme proteins in four-helix bundle scaffolds along with an analysis of the Protein Data Bank, we have investigated the various factors that modulate the ferric and ferrous heme affinity of protein ligands, and the resultant electrochemistry fundamental to the biological activity of cytochromes. Using detailed equilibria studies of a simple sixteen amino acid peptide that avidly binds Zn(II), we have developed a method to reveal the free energy cost of protein folding hidden in metal-induced protein folding effects of the zinc finger transcription factors. These studies provide insight these two important classes of metalloproteins and enhance our efforts at the rational design of metallproteins.

Coordination chemistry of designed metallopeptides: Insight into the biological function of natural metalloproteins

251st National Meeting (2016)

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