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

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Eurobic9, 2-6 September, 2008, Wrocław, Poland P109. Characterization and Reactivity of [Ru(β)(L)Cl2]ClO4 ( L= Tpea, Me6tpea ) J. E. Lee , J. H. Cho , H. I. Lee Department of Chemistry, Kyungpook National University, 1370 SangKyeok-Dong, 702-701, Deagu, Republic of Korea e-mail: jjuni32@hanmail.net We prepared Ru(III) complexes with tripodal, pyrazoyl ligand [Ru(β)(L)Cl2]ClO4 (L= Tpea 1, Me6tpea 2)]. Single crystal study identified octahedral geometry with tetradentate Tpea ligand and two chloride ions. Reactivity toward the oxidation of d-glucose and d-fructose by the complexes and hydrogen peroxide was investigated using UV-VIS and EPR, which showed that only 1 could oxidize the hexoses at pH 7 (0.01M phosphate). We describe the stabilization of high oxidation state and other properties. _____________________________________________________________________ 228
Eurobic9, 2-6 September, 2008, Wrocław, Poland P110. Oxygen Sensibility of Ni-Fe Hydrogenases with Modified Gas Channels F. Leroux a , S. Dementin a , B. Burlat a , A. Volbeda b , J. Fontecilla-Camps b , M. Rousset a , P. Bertrand a , B. Guigliarelli a , Ch. Léger a a Laboratoire de Bioénergétique et Ingénierie des, CNRS - Université de Provence, 31 chemin Jospeh Aiguier, 13402, Marseille Cedex 20, France, b Laboratoire de Cristallographie et Cristallogenès, CEA, Grenoble, France e-mail: fanny.leroux@ibsm.cnrs-mrs.fr Hydrogenases catalyze the conversion between H2 and H+ as part of the bioenergetic metabolism of most bacteria. The main obstacle for their use as catalysts in biofuel cells is the fact that they are inhibited by molecular oxygen [1]. The active site of the so-called Ni-Fe hydrogenase is buried in the protein. Structural and molecular dynamic studies suggest that a hydrophobic channel guides hydrogen and inhibitors towards the active site and recent results suggest that the shape of this tunnel may determine the sensitivity to oxygen [2]. We introduce a quantitative experimental method for probing the rates of intra-molecular diffusion within hydrogenases based on using Protein Film Voltammetry, a technique where enzymes molecules are adsorbed on an electrode, a potential is applied and the resulting current is proportional to enzyme's activity [3-4]. We use it to resolve the kinetics of binding and release of the competitive inhibitor CO and of the reaction with O2 [5-6]. We study how the structure of the channel affects the diffusion of CO and the rate of O2 inhibition in several mutants whose structures have been determined. We will show that certain mutations slow down gas diffusion [7] and affect the sensitivity of the enzyme. However, CO always reacts with the enzyme much faster than O2 does, this implies that intramolecular transport does not limit the rate of oxygen inhibition, at least in the WT enzyme. References: [1] De Lacey, Fernandez, Rousset, Cammack, Chem. Rev. 2007, 107 (10), 4304-30. [2] Buhrke, Lenz, Krauss, Friedrich, J. Biol. Chem. 2005, 23791. [3] Léger, Elliott, Hoke, Jeuken, Jones, Armstrong, Biochemistry, 2003, 42, 8653. [4] Léger, Bertrand, Chem Rev, in press (july 2008). [5] Léger, Dementin, Bertrand, Rousset, Guigliarelli, J. Am. Chem. Soc., 126, 2004, 38. [6] Baffert, Demuez, Cournac, Burlat, Guigliarelli, Bertrand, Girbal, Léger, Angew. Chem. Int. Ed. 47, 2008, 2052. [7] Leroux, Dementin, Burlat, Cournac, Volbeda, Champ, Martin, Guigliarelli, Bertrand, Fontecilla-Camps, Rousset, Léger, submitted. _____________________________________________________________________ 229
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ISBN: 978-83-60043-10-3 - eurobic9

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