ISBN: 978-83-60043-10-3 - eurobic9

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Eurobic9, 2-6 September, 2008, Wrocław, Poland P175. A Novel Paddlewheel Dicopper(II) Molecule with Four µ2-N3,N7- [N1,N6-dideaza-adeninate(1-)] Bridges C. Sánchez de Medina-Revilla a , D. Choquesillo-Lazarte b , A. Domínguez-Martín a , J.M. González-Pérez a , A. Castiñeiras c , J. Niclós-Gutiérrez a a Department of Inorganic Chemistry, University of Granada, Fac. Pharmacy, Campus Cartuja, E-18071 Granada, Spain e-mail: celiasm@ugr.es b Laboratorio de Estudios Cristalográficos, IACT-CSIC, Edif. Inst Lopez-Neyra, PTCS. Avda. del Conocimiento s/n, E-18<strong>10</strong>0 Armilla, Granada, Spain c Department of Inorganic Chemistry, University of Santiago, Fac. Pharmacy, Campus Sur, E-15782 Santiago de Compostela, Spain The adeninate(1-) ion has probed to act as and µ-N3,N7,N9-bridging ligand, in an hexanuclear molecule [1] and in a polymer [2]. Such a role would be displayed by 4-azabencimidazolate(1-) [also N1,N6-dideazaadeninate(1-), 4abim - ], but without a N6-H···A interaction reinforcing a metal-N7 bond. Reedijk et al. [3] have reported the structure of [Cu2(µ2-N3,N7-4abim)4X2]X2·solvated salts (X = Cl or Br) and studied their strongly anti-ferromagnetic coupling behaviour. Now we inform of the closely related paddlewheel centro-symmetric molecule [Cu2(µ2-N3,N7-4abim)4(SO4)2]·12H2O (293 K, monoclinic, space group C2/c, final R 0.056,see figure). Relevant inter-atomic distances (Å): Cu···Cu 2.960(1), Cu-N3 2.019(3), Cu-N9 2.016(3), Cu-O(sulphate) 2.113(14). In the crystal, pairs of H-bonding interactions N7-H···O(sulphate) give chains. References: [1] J.M. González-Pérez, C. Alarcón-Payer, A. Castiñeiras, T. Pivetta, L. Lezama, D. Choquesillo-Lazarte, G. Crisponi, J. Niclós-Gutiérrez, Inorg. Chem., 45, 877 (2006). [2] J.P. García Terán, O. Castillo, A. Luque, U. García Cruceiro, P. Román, Inorg. Chem., 43, 4549 (2004). [3] G.A. van Albada, I. Mutikainen, U. Turpeinen, J. Reedijk, Polyhedron, 25, 3278 (2006). _____________________________________________________________________ 294
Eurobic9, 2-6 September, 2008, Wrocław, Poland P176. Structural Studies on Desulfoviridin from Desulfovibrio desulfuricans ATCC 27774 A.S. Serra a , M. Carepo a , S.L.A. Andrade b , I. Moura a , J.J.G. Moura a and M.G. Almeida a REQUIMTE / CQFB, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Quinta da Torre, 2829-516 Caparica, Portugal b Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany c Escola Superior de Saúde Egas Moniz, Quinta da Granja, Monte de Caparica, 2829-511 Caparica, Portugal Desulfoviridin (Dsv) is a dissimilatory sulfite reductase capable of reducing sulfite to sulfide during anaerobic respiration. A detailed knowledge of the enzyme’s multimeric (α2β2γ2) structure from Desulfovibrio genus is not available, and it is our goal to carry out such characterization using Dsv from Desulfovibrio desulfuricans ATCC 27774 cells. The molecular mass of the native protein as obtained from gel filtration chromatography, compared with the molecular mass and intensity of the corresponding bands identified by SDS-PAGE (9, 35, 49 kDa), indicates that Dsv is purified as a α2β2γ2 complex. The total and free iron content is in agreement with the existence of two sirohaems and four [Fe4S4] clusters. For obtaining the complete sequence of Dsv subunits (α, β and γ), primers were designed for DNA amplification by PCR, based on multiple sequence alignments of dsr genes from several Desulfovibrio species and N-terminal chemical sequencing of the subunits. The sequences obtained were compared with deposited homologous sequences as well as with D. desulfuricans internal peptide sequences obtained after enzymatic digestion. In order to use X-ray diffraction techniques to solve the crystallographic structure of D. desulfuricans Desulfoviridin, preliminary screenings were made yielding small protein crystals. The refinement of the crystallization conditions is currently under optimization. References: [1] Steuber, J. et al; Eur.J.Biochem.; 1995; 233; 873-879 [2] Marritt, S. J.; Hagen, W. R.; Eur.J.Biochem.; 1996; 238; 724-727 [3] Mander, G. J. et al; FEBS Let.; 2005, 579, 4600-4604 [4] Schiffer, A. et al; Journal of Molecular Biology; 2008; in press _____________________________________________________________________ 295 a, c
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ISBN: 978-83-60043-10-3 - eurobic9

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