Hydrogen Bonded Phenols as Models for Redox-Active Tyrosines in Enzymes

University dissertation from Stockholm : Institutionen för organisk kemi

Abstract: This thesis deals with the impact of hydrogen bonding on the properties of phenols. The possibility for tyrosine to form hydrogen bonds to other amino acids has been found to be important for its function as an electron transfer mediator in a number of important redox enzymes. This study has focused on modeling the function of tyrosine in Photosystem II, a crucial enzyme in the photosynthetic pathway of green plants.Hydrogen bonds between phenol and amines in both inter- and intramolecular systems have been studied with quantum chemical calculations and also in some solid-state structures involving phenol and imidazole.Different phenols linked to amines have been synthesized and their possibilities of forming intra- and intermolecular hydrogen bonds have been studied as well as the thermodynamics and kinetics of the generation of phenoxyl radicals via oxidation reactions.Since carboxylates may in principle act as hydrogen bond acceptors in a manner similar to imidazole, proton coupled electron transfer has also been studied for a few phenols intramolecularly hydrogen bonded to carboxylates with the aim to elucidate the mechanism for oxidation. Electron transfer in a new linked phenol—ruthenium(II)trisbipyridine complex was studied as well.The knowledge is important for the ultimate goal of the project, which is to transform solar energy into a fuel by an artificial mimic of the natural photosynthetic apparatus