Hydrogen transfer in the presence of amino acid radicals

Abstract.

Quantum chemical model studies of hydrogen transfer between amino acids in the presence of radicals have been performed using the density functional theory method B3LYP. These studies were made to investigate alternative mechanisms to the conventional electron transfer-proton transfer mechanisms. The model reactions studied are such that the net result of the reaction is a transfer of one neutral hydrogen atom. Simple models are used for the amino acids. Three different mechanisms for hydrogen transfer were found. In the first of these, a transition state with a protonated intermediate residue is found, in the second, the proton and electron take different paths and in the third, a neutral hydrogen atom can be identified along the reaction pathway. A key feature of these mechanisms is that charge separation is always kept small in contrast to the previous electron transfer-proton transfer mechanisms. It is therefore proposed that the processes normally considered as electron transfer in the biochemical literature could in fact be better explained as hydrogen atom transfer, at least in cases where a suitable hydrogen bonded chain pathway is present in the protein. The presence of such chains in principle allows the protein to define the path of net hydrogen transfer. Another important conclusion is that standard quantum chemical methods can be used to treat these mechanisms for hydrogen transfer, allowing for an accurate representation of the geometric changes during the reactions.