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Bioinorganic Chemistry (bioinorganic + chemistry)
Selected AbstractsComputational Inorganic and Bioinorganic Chemistry.ANGEWANDTE CHEMIE, Issue 18 2010Herausgegeben von Edward John Wiley & Sons, Hoboken 2009. 614,S., geb., 155.00,,.,ISBN 978-0470699973 [source] Bioinorganic Chemistry: A Practical Course.ANGEWANDTE CHEMIE, Issue 13 2010Von Nils Metzler-Nolte und Ulrich Schatzschneider. De Gruyter, Berlin 2009. 138,S., Broschur, 44.95,,.,ISBN 978-3110209549 [source] Kazuo Nakamoto Infrared and Raman Spectra of Inorganic and Coordination Compounds, Part B, Applications in Coordination, Organometallic, and Bioinorganic Chemistry, 6th edn Wiley, 2009, 424 pp. (hardback) ISBN 978-0-471-74493-1APPLIED ORGANOMETALLIC CHEMISTRY, Issue 6 2010Alan Brisdon No abstract is available for this article. [source] Editorial: Topics in Bioinorganic ChemistryCHEMISTRY & BIODIVERSITY, Issue 8 2008Bernhard Keppler No abstract is available for this article. [source] Metal,thiolate bonds in bioinorganic chemistryJOURNAL OF COMPUTATIONAL CHEMISTRY, Issue 12 2006Edward I. Solomon Abstract Metal,thiolate active sites play major roles in bioinorganic chemistry. The MSthiolate bonds can be very covalent, and involve different orbital interactions. Spectroscopic features of these active sites (intense, low-energy charge transfer transitions) reflect the high covalency of the MSthiolate bonds. The energy of the metal,thiolate bond is fairly insensitive to its ionic/covalent and ,/, nature as increasing MS covalency reduces the charge distribution, hence the ionic term, and these contributions can compensate. Thus, trends observed in stability constants (i.e., the Irving,Williams series) mostly reflect the dominantly ionic contribution to bonding of the innocent ligand being replaced by the thiolate. Due to high effective nuclear charges of the CuII and FeIII ions, the cupric, and ferric,thiolate bonds are very covalent, with the former having strong , and the latter having more , character. For the blue copper site, the high , covalency couples the metal ion into the protein for rapid directional long range electron transfer. For rubredoxins, because the redox active molecular orbital is , in nature, electron transfer tends to be more localized in the vicinity of the active site. Although the energy of hydrogen bonding of the protein environment to the thiolate ligands tends to be fairly small, H-bonding can significantly affect the covalency of the metal,thiolate bond and contribute to redox tuning by the protein environment. © 2006 Wiley Periodicals, Inc. J Comput Chem 27: 1415,1428, 2006 [source] A Novel Tripodal Ligand Containing Three Different N -Heterocyclic Donor Functions and Its Application in Catechol Dioxygenase MimickingCHEMISTRY - A EUROPEAN JOURNAL, Issue 22 2009Marit Wagner Dipl.-Chem. Abstract Prominent donors: A pyridyl, an imidazolyl, and a pyrazolyl donor function are part of the novel tripodal ligand depicted, which thus combines three of the most prominent donors applied in ligands for bioinorganic chemistry within one coordination unit. To exploit its behaviour and potential, first investigations have been carried out in relation to catechol dioxygenase mimicry. We describe a novel chiral ligand, L, in which three different N -donor functions are linked to a methoxymethine unit: a methylpyrazole derivative, a methylimidazole unit, and a pyridyl residue. Complexes with FeCl2, FeBr2, and FeCl3 have been synthesized and fully characterized, including with respect to their molecular structures. While in combination with FeCl3L coordinates in a tripodal fashion, with FeX2 (X=Cl, Br) it binds only through two functions and the pyridyl unit remains dangling. For potential modelling of intradiol and extradiol catechol dioxygenase reactivity, the complexes [LFeCl2], 1, and [LFeCl3], 3, have been treated with 3,5-di- tert -butylcatechol, triethylamine, and O2. Both complexes yielded similar results in such investigations, since the LFeII,catecholate complex reacts with O2 through one-electron oxidation in the first step. Employing 3 in acetonitrile solution, intradiol cleavage occurred, although the undesired quinone was formed as the main product. If reagents were added (NaBPh4, H+) or reaction conditions were chosen (CH2Cl2 instead of CH3CN as the solvent) that made the coordination sphere at the iron centre more accessible for a third substrate donor function, an alternative reaction route, presumably involving O2 binding at the metal, became more important, which led to extradiol cleavage. In the extreme case (CH2Cl2 as the solvent and with the addition of NaBPh4), mainly the extradiol cleavage products were formed; the intradiol products were only observed as side products then and quinone formation became negligible. Protonated base functions in the second coordination sphere increased the efficiency of extradiol cleavage only slightly. The obtained results are in line with current understanding of the function of intradiol/extradiol dioxygenases. [source] | ||||||||||