Porphyrin is a very important component of natural and artificial catalysis and oxygen delivery in blood. Here, we report that, based on first-principles density-functional calculations, a hydrogenmolecule can be adsorbed non-dissociatively onto Ti-, V-, and Fe-porphyrins, similar to oxygenadsorption in heme-containing proteins, with a significant energy gain, greater than 0.3 eV per H2. The dihydrogen–heme complex will be non-magnetic, as is oxyhemoglobin. In contrast to the backward electron donation of Fe(III)–O2− in oxyhemoglobin, the dihydrogen binding originates from electron donation from H2 to the Fe(II). We have identified that the local symmetry of the transition metal center of porphyrins uniquely determines the binding strength, and, thus, one can even manipulate the strength by intentionally and systematically breaking symmetry.
http://www.rsc.org/Publishing/Journals/CP/article.asp?doi=b913711d
Covered by Phys. Chem. Phys. (Dec. 21, 2009) - Y. -H. Kim et al.
