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

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Eurobic9, 2-6 September, 2008, Wrocław, Poland P207. Photochemical Reduction of Nitrite Catalyzed by Ruthenium Complex or Zinc Porphyrin-linked Nitrite Reductases and the Model Cu Complexes K. Yamaguchi a , N. Isoda a , A. Tani a , T. Okada a , S. Suzuki a , N. Nakamura b , H. Ohno b , N. Ikeda a a Department of Chemistry, Grad. Sch. of Science, Osaka University, 1-1 Machikaneyama, 560-0043, Toyonaka, Osaka, Japan e-mail: kazu@ch.wani.osaka-u.ac.jp b Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei, 184-8588, Tokyo, Japan Copper-containing nitrite reductase (CuNIR), which is a key enzyme in biological denitrification, catalyzes the reduction of nitrite to nitrogen monoxide. In this paper, we investigated that and the photochemical reduction of nitrite to nitrogen monoxide by Ru(bpy)3 or Zn prophirin complex modified CuNIRs and the CuNIR model complexes [Cu(Me2bpa)] 2+ linked to Ru(bpy)3 analogue or Zn porphirin in the presence of sacrificial electron donor reagents under acidic condition at room temperature. Transient absorption spectra of Ru-Cu complex were observed by nanosecond laser flash photolysis (λex = 532 nm, fwhm 4 ns) at 298 K. The spectral change at 503 nm due to Ru(III) moiety was observed, it is due to the intramolecular electron transfer from the excited Ru(II) to Cu(II) moieties in Ru-Cu complex. The same profiles were observed in the Zn prophirin linked Cu complex and the Ru complex modified CuNIR. Photo chemical NO production from the dinuclear complexes or the complex modified CuNIR solutions including nitrite and sacrificial electron donor reagent was observed under irradiation of visible light and the continuous flow of Ar at room temperature. This is the first example of the photochemical reduction of nitrite to nitrogen monoxide catalyzed by dinuclear complex and complex modified enzyme. References: [1]K. Yamaguchi, T. Okada, and S. Suzuki, Inorganic Chemistry Commun., 9, 989-991 (2006). _____________________________________________________________________ 326
Eurobic9, 2-6 September, 2008, Wrocław, Poland P208. Reinvestigation of Dioxygen Activation by α-Ketoglutarate Dependent Dioxygenase S. Ye a , C. Riplinger a , C. Krebs b , M. Bollinger b , and F. Neese a a Institute of Physical and Theoretical Chemistry, Bonn University, Germany b Department of Biochemistry, Penn State University, USA The TauD/α-ketoglutarate (α-KG)-dependent dioxygenase is a member of the superfamily of α-ketoglutaratedependent dioxygenase, a large and diverse class of mononuclear non-heme iron enzymes that require hs-Fe(II), α-KG and dioxygen for catalysis. The reaction mechanism for dioxygen activation in this enzyme system has been studied by hybrid density functional theory (DFT) at septet, quintet and triplet potential energy surfaces. The calculations showed that the dioxygen activation proceeds at the septet potential surface through only one transition state for a concerted O-O and C-C bond cleavage, which is consistent with the experimental findings that oxidative decarboxylation of the α-KG is the rate-limiting step. Detailed analysis of the electron pathways for the four-electron reduction process of dioxygen provided new insights into the catalytic mechanism: Why is only one transition state needed at the septet surface? Why can the similar process not take place at the quintet and triplet potential surfaces? What kind of roles do the hs-Fe(II) and α-KG play for the dioxygen activation? _____________________________________________________________________ 327
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ISBN: 978-83-60043-10-3 - eurobic9

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