toppfinansiering til Fp7 People Marie Curie Action IEF grant Dr. Giorgio Zoppellaro

Marie Curie Action IEF grant Dr. Giorgio Zoppellaro need extra money to at least get Lønnstrinn 57 and 58. Dr. Giorgio Zoppellaro was earlier 2007-2008 at Lønnstrinn 57 at Univ of Oslo, but was forced down to Lønnstrinn 54 as an IEF, as founding is to low from a IEF MCA grant. The aim of the project is to investigate structural features of oxygen or electron reactions in proteins containing functionally important iron, and/or radical centers and compair with copper, manganese proteins. This type of d i-iron cluster can perform several different tasks, e.g., stabilize a tyrosyl radical in RNR-R2 (the smaller subunit, R2, of ribonucleotide reductase, RNR) or e.g. in other enzymes the cluster can be the site of mono-oxygenase/desaturase chemistry. We wi ll study di- or monooxygenases that can perform very difficult reactions. Other monooxygenases have large medical importance, e.g. tetrahydrobiopterin dependent monooxygenases/ heme proteins nitric oxide synthase (NOS) and AlkB, p53R2 in DNA repair. We p lan to study: 1) the radical in both subunits of RNR-R2 and R1 of proteins from mouse, human, fish, (posibly plant) and B. cereus; 2) nitric oxide synthases (NOS) 3) myoglobin/hemoglobin and other heme containing proteins will be studied; 4) mono nuclear iron dependet proteins will be compaired with di-nuclear proteins and with Mn, Co proteins; and 5) Copper proteins; RNR, NOS, AlkB, are cloned and expressed in E. coli and activity dependent mutants are made or will be obtained. We will study structur e & properties of the metallo- and radical centers of these proteins: long-term goal of understanding monooxygenase and radical chemistry important to make rational drug or modulator design. We are developing a combination of techniques for proteins in so lution and in crystal form. We have started EPR and resonance Raman studies of protein crystals. We continue to develop HF EPR of radicals and metal sites after irradiation, hypoxia.