Sulfilimine

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John W Gilje - One of the best experts on this subject based on the ideXlab platform.

  • uranium Sulfilimine chemistry synthesis and characterization of cp 2ucl nsph2 and cp 2u nsph2 2
    Organometallics, 2002
    Co-Authors: Kanahara A N S Ariyaratne, Roger E Cramer, John W Gilje
    Abstract:

    Two imido derivatives of U(IV), Cp*2UCl(NSPh2) (1; Cp* = pentamethylcyclopentadienyl) and Cp*2U(NSPh2)2 (2), have been prepared in high yield from Cp*2UCl2 and LiNSPh2. Alternatively, 1 and 2 can be synthesized by treating Cp*2UCl[(CH2)2PPh2] with anhydrous HNSPh2. Cp*2U(NSPh2)2 is the first structurally characterized uranium bis(sulfilimide) complex. Its short U−N distance suggests significant uranium−imido multiple-bond character.

  • Uranium−Sulfilimine Chemistry: Synthesis and Characterization of Cp*2UCl(NSPh2) and Cp*2U(NSPh2)2
    Organometallics, 2002
    Co-Authors: Kanahara A N S Ariyaratne, Roger E Cramer, John W Gilje
    Abstract:

    Two imido derivatives of U(IV), Cp*2UCl(NSPh2) (1; Cp* = pentamethylcyclopentadienyl) and Cp*2U(NSPh2)2 (2), have been prepared in high yield from Cp*2UCl2 and LiNSPh2. Alternatively, 1 and 2 can be synthesized by treating Cp*2UCl[(CH2)2PPh2] with anhydrous HNSPh2. Cp*2U(NSPh2)2 is the first structurally characterized uranium bis(sulfilimide) complex. Its short U−N distance suggests significant uranium−imido multiple-bond character.

  • uranium Sulfilimine chemistry the preparation of cp2 ucl2 hnsph2 and its hydrolysis with hnsph2 h2o
    Zeitschrift für anorganische und allgemeine Chemie, 1995
    Co-Authors: Roger E Cramer, K A N S Ariyaratne, John W Gilje
    Abstract:

    The reaction of Cp2*UCl2 with HNSPh2 produces Cp2*UCl2(HNSPh2), which is the first structurally characterized complex of a Sulfilimine. The hydrolysis of Cp2*UCl2(HNSPh2) with HNSPh2 · H2O yields a tetrauranium cluster whose heavy atom structure has been determined by x-ray diffraction and which is formulated as a UIV/UV complex: [Cp*(Cl)(HNSPh2)U(μ3-O)(μ2-O)2U(Cl)(HNSPh2)2]2. Uran-Sulfilimin-Chemie Darstellung von Cp2*UCl2(HNSPh2) und dessen Hydrolyse mit HNSPh2 · H2O Die Reaktion von Cp2*UCl2 mit HNSPh2 ergibt Cp2*UCl2(HNSPh2), das den ersten strukturell charakterisierten Komplex eines Sulfilimins darstellt. Die Hydrolyse von Cp2*UCl2(HNSPh2) mit HNSPh2 · H2O ergibt einen Tetrauran-Cluster, dessen Schweratomstruktur rontgenographisch bestimmt wurde und der als UIV/UV-Komplex [Cp*(Cl)(HNSPh2)U(μ3-O)(μ2-O)2U(Cl)(HNSPh2)2]2 formuliert wird.

  • Uranium‐Sulfilimine chemistry. The preparation of Cp2*UCl2(HNSPh2) and its hydrolysis with HNSPh2 · H2O
    Zeitschrift für anorganische und allgemeine Chemie, 1995
    Co-Authors: Roger E Cramer, K A N S Ariyaratne, John W Gilje
    Abstract:

    The reaction of Cp2*UCl2 with HNSPh2 produces Cp2*UCl2(HNSPh2), which is the first structurally characterized complex of a Sulfilimine. The hydrolysis of Cp2*UCl2(HNSPh2) with HNSPh2 · H2O yields a tetrauranium cluster whose heavy atom structure has been determined by x-ray diffraction and which is formulated as a UIV/UV complex: [Cp*(Cl)(HNSPh2)U(μ3-O)(μ2-O)2U(Cl)(HNSPh2)2]2. Uran-Sulfilimin-Chemie Darstellung von Cp2*UCl2(HNSPh2) und dessen Hydrolyse mit HNSPh2 · H2O Die Reaktion von Cp2*UCl2 mit HNSPh2 ergibt Cp2*UCl2(HNSPh2), das den ersten strukturell charakterisierten Komplex eines Sulfilimins darstellt. Die Hydrolyse von Cp2*UCl2(HNSPh2) mit HNSPh2 · H2O ergibt einen Tetrauran-Cluster, dessen Schweratomstruktur rontgenographisch bestimmt wurde und der als UIV/UV-Komplex [Cp*(Cl)(HNSPh2)U(μ3-O)(μ2-O)2U(Cl)(HNSPh2)2]2 formuliert wird.

Zigang Li - One of the best experts on this subject based on the ideXlab platform.

Carsten Bolm - One of the best experts on this subject based on the ideXlab platform.

Yixiang Jiang - One of the best experts on this subject based on the ideXlab platform.

Gautam Bhave - One of the best experts on this subject based on the ideXlab platform.

  • the ancient immunoglobulin domains of peroxidasin are required to form Sulfilimine cross links in collagen iv
    Journal of Biological Chemistry, 2015
    Co-Authors: Isi A Erotolliver, Billy G Hudson, Gautam Bhave
    Abstract:

    Abstract The collagen IV Sulfilimine cross-link and its catalyzing enzyme, peroxidasin, represent a dyad critical for tissue development, which is conserved throughout the animal kingdom. Peroxidasin forms novel Sulfilimine bonds between opposing methionine and hydroxylysine residues to structurally reinforce the collagen IV scaffold, a function critical for basement membrane and tissue integrity. However, the molecular mechanism underlying cross-link formation remains unclear. In this work, we demonstrate that the catalytic domain of peroxidasin and its immunoglobulin (Ig) domains are required for efficient Sulfilimine bond formation. Thus, these molecular features underlie the evolutionarily conserved function of peroxidasin in tissue development and integrity and distinguish peroxidasin from other peroxidases, such as myeloperoxidase (MPO) and eosinophil peroxidase (EPO).

  • Peroxidasin forms Sulfilimine chemical bonds using hypohalous acids in tissue genesis
    Nature Chemical Biology, 2012
    Co-Authors: Gautam Bhave, Christopher F Cummings, Roberto M Vanacore, Chino Kumagai-cresse, Isi A Ero-tolliver, Mohamed Rafi, Jeong-suk Kang, Vadim Pedchenko, Liselotte I Fessler, John H Fessler
    Abstract:

    Peroxidasin uses hypohalous acid oxidants to catalyze the formation of Sulfilimine bonds in basement membranes. Collagen IV comprises the predominant protein network of basement membranes, a specialized extracellular matrix, which underlie epithelia and endothelia. These networks assemble through oligomerization and covalent crosslinking to endow mechanical strength and shape cell behavior through interactions with cell-surface receptors. A recently discovered Sulfilimine (S=N) bond between a methionine sulfur and hydroxylysine nitrogen reinforces the collagen IV network. We demonstrate that peroxidasin, an enzyme found in basement membranes, catalyzes formation of the Sulfilimine bond. Drosophila peroxidasin mutants have disorganized collagen IV networks and torn visceral muscle basement membranes, pointing to a critical role for the enzyme in tissue biogenesis. Peroxidasin generates hypohalous acids as reaction intermediates, suggesting a paradoxically anabolic role for these usually destructive oxidants. This work highlights Sulfilimine bond formation as what is to our knowledge the first known physiologic function for peroxidasin, a role for hypohalous oxidants in tissue biogenesis, and a possible role for peroxidasin in inflammatory diseases.

  • peroxidasin forms Sulfilimine chemical bonds using hypohalous acids in tissue genesis
    Nature Chemical Biology, 2012
    Co-Authors: Gautam Bhave, Christopher F Cummings, Roberto M Vanacore, Mohamed Rafi, Jeong-suk Kang, Vadim Pedchenko, Liselotte I Fessler, Isi A Erotolliver, Chino Kumagaicresse, John H Fessler
    Abstract:

    Peroxidasin uses hypohalous acid oxidants to catalyze the formation of Sulfilimine bonds in basement membranes.

  • sulphilimine Sulfilimine cross links in goodpasture s disease
    Clinical and Experimental Immunology, 2011
    Co-Authors: Roberto M Vanacore, Gautam Bhave, Vadim Pedchenko, Billy G Hudson
    Abstract:

    Summary The sulphilimine/Sulfilimine cross-link of the Goodpasture (GP) autoantigen is a novel molecular mechanism (structural constraint) for conferring immune privilege to a site which otherwise is susceptible to structural changes that induce an immunogenic and pathogenic conformation. Perturbation of the assembly or cleavage of the sulphilimine/Sulfilimine cross-links could be a key factor in the aetiology of Goodpasture's disease in susceptible individuals.