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

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Eurobic9, 2-6 September, 2008, Wrocław, Poland P129. Selenium, Tellurium and Transition Metals as Chemical Ingredients of Intelligent Antioxidants H. Mohammed a , S. Mecklenburg a , M. Doering a , S. Shaaban a , T. Burkholz a , C. Collins b , M. Abbas a , A. Anwar a , C. Jacob Claus a a Bioorganic Chemistry, University of Saarland, University Campus, 66123, Saarbruecken, Germany, b School of Biological and Chemical Sciences, University of Exeter, Stocker Road, Exeter, UK e-mail: h.mohammed@mx.uni-saarland.de Elements such as selenium and tellurium are generally not too popular in Bioinorganic Chemistry. Nonetheless, the combination of selenium, tellurium and various transition metal ions in chemically simple molecules provides a successful recipe for powerful pro- and antioxidants, which may be further ‘spiced' by the addition of organic redox centres [1, 2]. Antioxidants are used against oxidative stress (OS), a disturbance in redox homeostasis associated with numerous human diseases. Importantly, OS is not a single molecule event, but is associated with the increase in intracellular concentrations of various reactive, oxidizing species, and loss of antioxidant defence. Since reactive oxygen species (ROS), iron and copper ions are among the major culprits causing and propagating OS, we have considered the design of multifunctional molecules which combine the ability to remove ROS and bind (and disarm) adventitious metal ions [2]. These molecules are synthesised using various synthetic techniques, including multicomponent reactions and integrate one or more sulfur, selenium and tellurium redox centres with macrocycles, phenolic and quinone-based redox sites [3]. They exhibit an exciting electrochemical behaviour and bind/exchange zinc, copper and iron ions [1]. They are catalytically active and, when tested in skin cell culture, show strong antioxidant effects, probably due to catalytic destruction of ROS and exchange of beneficial zinc ions for toxic copper/iron ions. References: [1] Mecklenburg, S.; Collins, C. A.; Doring, M.; Burkholz, T.; Abbas, M.; Fry, F. H.; Pourzand, C.; Jacob, C. Phosphorus Sulfur and Silicon and the Related Elements 2008, 183 (4), 863-88. [2] Collins, C. A.; Fry, F. H.; Holme, A. L.; Yiakouvaki, A.; Al-Qenaei, A.; Pourzand, C.; Jacob, C. Org. Biomol. Chem. 2005, 3 (8), 1541-1546. [3] Shabaan, S.; Abbas, M.; Jacob, C. 2008, Manuscript in preparation. _____________________________________________________________________ 248
Eurobic9, 2-6 September, 2008, Wrocław, Poland P130. Mo and W Containing Formate Dehydrogenases: Structural and Biochemical Characterization C. Mota a , M.G. Rivas a , P.J. Gonzalez a , C.D. Brondino b , J.J.G. Moura a , I. Moura a a REQUIMTE/CQFB - Departamento de Química, Faculdade de Ciências e Tecnologia - UNL, Quinta da Torre, 2829-516, Caparica, Portugal, b Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas -UN, Barrio El Pozo, 3000, Santa Fe, Argentina e-mail: cristianomota@dq.fct.unl.pt Formate dehydrogenases (Fdh) belong to the DMSO reductase family and catalyze the two electron oxidation of formate to carbon dioxide via a cleavage of the C-H bond [1]. The oxidized active site of these enzymes can contain a hexacoordinated molybdenum or tungsten atom [2, 3, 4]. The reaction mechanism of these enzymes seems to involve pentacoordinated or hexacoordinated species in presence or absence of inhibitors, respectively [5, 6]. The present work reports biochemical and EPR studies of a Mo- and a W-Fdh isolated from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio gigas, respectively. The main aim is to compare the catalytic properties of these enzymes to evaluate the relevance of the metal in the active site. References: [1] Khangulov S. V., Gladyshev V. N., Dismukes G. C., Stadtman T. C. Biochemistry 37 (1998), 3518-3528. [2] H. Raaijmakers, S. Macieira, J.M. Dias, S. Teixeira, S. Bursakov, R. Huber, J.J. Moura, I. Moura, M.J. Romao. Structure 10 (2002) 1261-1272. [3] M. Jormakka, S. Tornroth, B. Byrne, S. Iwata. Science 295 (2002) 1863-1868. [4] M. Jormakka, S. Tornroth, J. Abramson, B. Byrne, S. Iwata. Acta Crystallogr. D. Biol. Crystallogr. 58 (2002) 160-162. [5] J.C. Boyington, V.N. Gladyshev, S.V. Khangulov, T.C. Stadtman, P.D. Sun. Science 275 (1997) 1305-1308. [6] M.G. Rivas, P.J. González, C.D. Brondino, J.J.G. Moura, I. Moura. J. Inorg. Biochem. 101 (2007) (11-12):1617-1622. _____________________________________________________________________ 249
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ISBN: 978-83-60043-10-3 - eurobic9

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