Thesis supervisor: József Kaizer
Location of studies (in Hungarian): Department of Chemistry, University of Pannonia, Veszprém Abbreviation of location of studies: PE-DC
Description of the research topic:
Biological oxidation reactions utilizing dioxygen are amongst the most frequent reactions that occur in biology, where they are catalyzed by oxidoreductases. Model chemistry in relevance to metalloenzymes has progressed remarkably in recent years, and contributed greatly to clarification of structure and mechanism of various enzymes. The other important contribution of the model systems to the progress in enzymatic studies is to obtain information about structures and reactivities of substrate-metal intermediates, and investigate how the model chemistry is related to development of efficient catalysis by metal complexes. The aim of this project is to work out structural and functional models for the mononuclear (Taurin dioxygenase, ACC oxidase), and binuclear (Methane monooxygenase, Ribonucleotide reductase) non-heme Fe(II) enzymes to elucidate the catalytic pathways, mechanisms, and expand of chemistry from bioinorganic chemistry to bioinspired catalysis. On the bases of structural and functional models discussed above selective oxidations such as mono- and dioxygenations, olefin epoxidation, stereoselective alkane hydroxylation, and oxidative coupling reactions can be carried out in organic medium, which may have medical, pharmaceutical or agricultural significance. The correlation between the structure of the catalyst, and the efficiency, chemo-, regio-and enantioselectivity of their catalytic process will be investigated to make industrial processes more economically efficient with a higher productivity.
Required language skills: english Further requirements: MSc in Chemical Engineering or Chemistry