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Identifier uch.chemistry.msc//2005charalampidis
Title Πρόδρομες Ενώσεις για Βιομιμητικά Μοντέλα Κυτοχρωμικής c Οξειδάσης
Creator Charalampidis, Giorgos
Abstract Cytochrome c oxidase is an important porphyrin-containing enzyme, that catalyzes the four-electron (4e-), four-proton (4H+) reduction of O2 to H2O. The resulting energy is used to generate ATP as protons flow back through the membrane via ATP synthase. The structure of its active site is well known thanks to X-ray crystallography. Nonetheless, many issues such as the roles of copper CuB and Tyr residue in O2 binding, and reduction remain subjects of debate. In order to better understand the catalytic mechanism it is important to synthesize model compounds that closely resemble the native enzyme active sites. In this study novel porphyrins 1, 2 have been prepared as model compounds of cytochrome c oxidase active site, bearing a tyrosine molecule covalently attached to the porphyrin ring. The synthesis of porphyrin 1 involved the condensation reaction of nitrobenzaldehyde and dipyrromethane bearing bulky groups, in order to facilitate the separation of α,α- and α,β-atropisomers. Then a pyridine based ligand (potential copper binding site) and a tyrosine molecule were attached via amide bonds to the central scaffold. On the other hand, porphyrin 2 was synthesized using α,α,α,α-isomer of the aminoporphyrin as a template. N,N,N-tribenzyl-tris(aminoethyl)amine and a tyrosine molecule were attached to the aminoporphyrin via urea and amide bonds respectively.
Issue date 2005-04-01
Date available 2007-02-09
Collection   School/Department--School of Sciences and Engineering--Department of Chemistry--Post-graduate theses
  Type of Work--Post-graduate theses
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