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192ICM ICBIC Posters Journal of Inorganic Biochemistry 96 (2003) 203 Monomeric TpPrMoVOSR complexes via the chemical reduction of TpPrMoVIOSR. David J Nielsen, School of Chemistry, University of Melbourne, Australia Christian J Doonan, School of Chemistry, University of Melbourne, Australia Graham N George, Stanford Synchrotron Radiation Laboratory, United States Hugh Harris, Stanford Synchrotron Radiation Laboratory, United States Charles G Young, University of Melbourne, Australia EPR evidence has suggested the presence of molybdenum(V) intermediates in the catalytic cycle of hydroxylase enzyme systems [1], and references therein], and as such these species are attractive targets for the synthesis of small-molecule model systems. Ongoing work in our group has allowed access to several stable and well characterised monomeric molybdenum(VI) oxo-thio complexes TpPrMoVIOSR (TpPr = hydridotris(3-isopropylpyrazol-1-yl)borate) with co-ligand R = eg. substituted phenolates [2], as shown below. These Mo(VI) complexes have proved amenable to chemical reduction using cobaltocene (CoCp2) yielding initially the Pr V [CoCp2][Tp Mo OSR] salts [1,2]. Solution and solid state sulfur X-ray absorption spectroscopy (XAS) on selected examples of the chemically reduced species shows pre-edge features attributable to the S 1s → Mo=S π* transition of a [MoOS]+ unit. Further spectroscopic investigations (EPR, IR) are consistent with the presence of a paramagnetic Mo(V) centre bearing a terminal thio ligand. Continuing spectroscopic, structural and reactivity investigations centred on these important species will be presented. References: [1] P. D. Smith, D. A. Slizys, G. N. George and C. G. Young, J. Amer. Chem. Soc., 122(12), 2000, 2946. [2] C. J. Doonan, Unpublished results. 204 Journal of Inorganic Biochemistry 96 (2003) Nine-Zinc Finger Protein: Infl uence of TFIIIA-Type Linker at N- or C-Terminal on DNA Binding Site Wataru Nomura, Institute for Chemical Research, Kyoto University, Japan Yukio Sugiura, Institute for Chemical Research, Kyoto University, Japan In natural zinc fi nger proteins, the short linker sequence, Thr-Gly-Glu-Lys-Pro, is the most typical linkr sequence between each fi nger domain. Zinc fi nger proteins recognize specifi c DNA sequence by locating its α-helix in the major groove of DNA. The utilization of zinc fi nger proteins for the DNA sequence recognition has been investigated from the recognition helix experiments. The central three-zinc fi nger connection of the native nine-zinc fi nger protein transcription factor IIIA(TFIIIA) is composed of unique linker sequences, -NIKICV-, -TQQLP-, -AG-, and -QDL-. As revealed by X-ray crystallographic study of TFIIIA-5S rRNA gene complex, the characteristic DNA binding mode of TFIIIA zinc fi nger protein is brought from the unique linker sequences. By modifi cation of the linker sequences and adjustment of the linker length, several efforts to improve the DNA binding affi nity have been performed. However, it is unknown whether the position of the linker sequences in multi-zinc fi nger protein gives any effect on DNA bindings or not. New artifi cial nine-zinc fi nger proteins, Sp1ZF9TC and Sp1ZF9TN, which use TFIIIA-type linker for their C- and N- terminal three-zinc fi nger connections have been created. To investigate the infl uence of TFIIIA-type linker by their different locations in the proteins, the gel mobility shift assays(GMSA), footprinting assays, and methylation interference analyses were performed.The GMSA revealed similar DNA binding affi nities of the two proteins. The footprinting analyses indicated that the two zinc fi nger proteins recognize the same part of GCII or GCIII DNA. Moreover, the specifi c base contacts were observed in the same sites of the substrate DNA. In the present proteins, Sp1ZF9TC and Sp1ZF9TN, the four zinc fi ngers (the fi ngers 1~4 or 5~9) situated in the opposite site to the TFIIIA-linker position participate in their DNA bindings. Indeed, the position of TFIIIA-linker is important in DNA recognition by multi-zinc fi nger proteins. Reaction mechanism of nitrile hydratase: analysis by isobutryronitrile Masafumi Odaka, Bioengineering Laboratory, RIKEN, Japan Masanari Tsujimura, Bioengineering Laboratory, RIKEN, Japan Hiroshi Nakayama, Biomolecular Charactrization Division, RIKEN, Japan Naoshi Dohmae, Biomolecular Charactrization Division, RIKEN, Japan Mikio Hoshino, Synthetic Organic Chemistry Laboratory, RIKEN, Japan Koji Takio, Biomolecular Charactrization Division, RIKEN, Japan Mizuo Maeda, Bioengineering Laboratory, RIKEN, Japan Isao Endo, Faculty of Agriculture, Utsunomiya University, Japan Nitrile hydratase (NHase) catalyzing the hydration of nitriles to the corresponding amides is industrially important because of the production of acrylamide. NHase is a non-heme iron or non-corrin cobalt enzyme. Recent X-ray crystallographic analyses demonstrated that the structures around the catalytic center were conserved between Fe- and Co-type NHases including two post-translationally modifi ed cysteine ligands, cysteine-sulfi nic (Cys-SO2H) and -sulfenic acids (Cys-SOH). These modifi cations are believed to be responsible for the catalytic reaction. However, the detailed reaction mechanism remains unknown. In general, NHase exhibits wide substrate specifi city. It is of interest that isobutyronitrile (IBN) was known to barely hydrated and to function as a competitive inhibitor of Fe-type NHases of two bacterial strains with Ki values of about 5 µM. These fi ndings sound curious because n-butyronitrile is normally hydrated by these enzymes and because Fe- type NHases of other strains hydrate IBN with relatively slow rate constant. Thus, we have studied the interaction between isobutyronitrile (IBN) and Fe-type NHase in detail. From kinetic studies of the inhibitory effect of IBN on NHase, we found that commercially available IBN contained an unknown compound that strongly inhibited NHase activity. This compound induced signifi cant changes on the UV-Vis absorption spectrum of NHase, suggesting its interaction with the iron center. The compound was isolated by reversed-phase HPLC and identifi ed as 2-cyano-2-propyl hydroperoxide (Cpx) by NMR. Upon the addition of stoichiometric amount of Cpx, NHase was irreversibly inactivated, probably by the oxidation of the Cys-SOH ligand to Cys-SO2H (NHase(double sulfi nate)). Moreover, UV-Vis absorption spectral changes of NHase induced by Cpx suggested that Cpx was associated with NHase(double sulfi nate), to form a stable complex. Cpx is a novel inhibitor for Fe-NHase and gives a clue for understanding its catalytic mechanism. Journal of Inorganic Biochemistry 96 (2003) 205 Expression and spectroscopic characterization of Pseudomonas ovalis [2Fe-2S] ferredoxin involved in the iron-sulfur cluster assembly machinery Daijiro Ohmori, Department of Chemistry, School of Medicine, Juntendo University, Japan Takeo Imai, Department of Life Science, Rikkyo University, Japan Akio Urushiyama, Department of Chemistry, Rikkyo University, Japan Minoru Akiyama, Department of Chemistry, Rikkyo University, Japan Eiji Watanabe, Department of Chemistry, School of Medicine, Juntendo University, Japan Fumiyuki Yamakura, Department of Chemistry, School of Medicine, Juntendo University, Japan Keikichi Uchida, Department of Biology, School of Medicine, Juntendo University, Japan We reported that Pseudomonas ovalis contained two types of ferredoxins; 7Fe-ferredoxin and 2Fe-ferredoxin. To investigate detailed features and physiological roles, we cloned the genes encoding 2Fe-ferredoxin(fdxB) from the chromosomal DNA of P. ovalis . The two ORF translations upstream of fdxB has a similarity to the heat shock protein family, hscA and a part of hscB, those are members of the iron-sulfur cluster assembly gene cluster. The fdxB translation has a signifi cant similarity to the primary structures of E. coli 2Fe-ferredoxin, which is involved in the iron-sulfur cluster assembly machinery. The UV-vis absorption spectrum of the recombinant ferredoxin reveals a characteristic feature of [2Fe-2S] ferredoxins. Circular dichroism spectra of the oxidized and reduced protein were similar to those of vertebrate-type ferredoxins than to those of plat-type ferredoxins. The 77K Resonance Raman spectrum of the protein in the Fe-S stretching region displays closely similar band frequencies (287, 317, 327, 332, 350, 394, 421cm-1) to that of bovine adrenodoxin, though it displays signifi cantly different band frequencies from those of spinach ferredoixn-I and ferredoxin-II. EPR spectrum of the reduced protein exhibits an axially symmetric spectrum (g1=2.02, g2=1.94), which is more similar to that of adrenodoxin than that of spinach ferredoxin-I (rhombic symmetry spectrum). These spectroscopic data imply that the [2Fe-2S] cluster environment in the protein is similar to that of a vertebrate-type ferredoxin. Effi cient N-terminal Peptide Sequencing using Bis(terpyridine)Ruthenium(II) Derivatives Taka-aki Okamura, Osaka University, Japan Norikazu Ueryama, Osaka University, Japan Taku Iwamura, Osaka University, Japan Mana Ikemori, Osaka University, Japan Maki Kaneko, Osaka University, Japan Ken Masui, Osaka University, Japan Hitoshi Yamamoto, Osaka University, Japan Minoru Yamaguchi, Shimadzu Corporation, Japan Hiroki Kuyama, Shimadzu Corporation, Japan Eiji Ando, Shimadzu Corporation, Japan Susumu Tsunasawa, Shimadzu Corporation, Japan Proteomics has become one of the most important projects in biological and medical fi elds. For exhaustive identifi cation of proteins in each organism, speedy and powerful analytical
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