8 research outputs found
Structural studies of organic and inorganic compounds
EThOS - Electronic Theses Online ServiceGBUnited Kingdo
Diaquabis(cinnamato-κ2O,O′)cadmium
The title complex, [Cd(C9H7O2)2(H2O)2], was obtained as an unintended product of the reaction of cadmium nitrate with hexamethylenetetramine and cinnamic acid. The CdII ion lies on a twofold rotation axis and is coordinated in a slightly distorted trigonal–prismatic environment. In the crystal, the V-shaped molecules are arranged in an interlocking fashion along [010] and O—H...O hydrogen bonds link the molecules, forming a two-dimensional network parallel to (001)
Intermediates in the synthesis of nitrogen heterocycles:addition of acylated camphorsultams to nitroalkenes
Thiolates vs. halides as π-donors: the redox-active alkyne complexes [M(SR)L(η-R′CCR′)L′] {M = Mo or W, L = CO or P(OMe)3, L′ = η-C5H5 and Tp′}
Synthesis, crystal structure, luminescent properties and antibacterial activities of zinc complexes with bipyridyl and salicylate ligands
Phosphate ester cleavage promoted by a tetrameric iron(III) complex
The purple acid phosphatases (PAPs) are the only binuclear metallohydrolases where the necessity for a heterovalent active site [Fe(III)-M(II) (M is Fe, Zn or Mn)] for catalysis has been established. The paradigm for the construction of PAP biomimetics, both structural and functional, is that the ligands possess characteristics which mimic those of the donor sites of the metalloenzyme and permit discrimination between trivalent and divalent metal ions. The donor atom set of the ligand 2-((2-hydroxy-5-methyl-3-((pyridin-2-ylmethylamino)methyl)benzyl) (2-hydroxybenzyl)amino)acetic acid (H(3)HPBA) mimics that of the active site of PAP although the iron(III) complex of this ligand has been characterized as the tetramer [Fe(4)(HPBA)(2)(mu-CH(3)COO)(2)(mu-O)(mu-OH)(OH(2))(2)]ClO(4)center dot 5H(2)O. The phosphoesterase-like activity of the complex in 1:1 acetonitrile/water has now been investigated using the substrate 2,4-bis(dinitrophenyl)phosphate. The pH dependence of the catalytic rate revealed a non-symmetric bell-shaped profile, with a finite but non-zero rate at high pH. Unlike the traditional approach usually employed to analyse these bell-shaped profiles, the approach used here involved incorporating additional species which contribute to the overall activity. Employing this approach, we show that the complex has a k(cat) of 1.6 (+/- 0.2) x 10(-3) s(-1), three kinetically relevant pK(a) values of 5.3, 6.2 and 8.4, with K(M) of 7.4 +/- 0.6 mM. The kinetic parameters are similar to those reported for heterovalent PAP biomimetics. Additionally, it is observed that, unlike the enzyme, the oxidation state is not the determining factor for catalytic activity