Why iron? A spin-polarized conceptual density functional theory study on metal-binding specificity of porphyrin

Heme is a key cofactor of hemoproteins in which porphyrin is often found to be preferentially metalated by the iron cation. In our previous work [Feng, X. T.; Yu, J. G.; Lei, M.; Fang, W. H.; Liu, S. B. J. Phys. Chem. B 2009, 113, 13381], conceptual density functional theory (CDFT) descriptors have been applied to understand the metal-binding specificity of porphyrin. We found that the iron-porphyrin complex significantly differs in many aspects from porphyrin complexes with other metal cations except Ru, for which similar behaviors for the reactivity descriptors were discovered. In this study, we employ the spin-polarized version of CDFT to investigate the reactivity for a series of (pyridine)(n)-M(ll)-porphyrin complexes-where M = Mg, Ca, Cr, Mn, Co, Ni, Cu, Zn, Ru, and Cd, and n = 0, 1, and 2-to further appreciate the metal-binding specificity of porphyrin. Both global and local descriptors were examined within this framework. We found that, within the spin resolution, not only chemical reactivity descriptors from CDFT of the iron complex are markedly different from that of other metal complexes, but we also discovered substantial differences in reactivity descriptors between Fe and Ru complexes. These results confirm that spin properties play a highly important role in physiological functions of hemoproteins. Quantitative reactivity relationships have been revealed between global and local spin-polarized reactivity descriptors. These results contribute to our better understanding of the metal binding specificity and reactivity for heme-containing enzymes and other metalloproteins alike.