ABSTRACT
The ligands bis(8-quinolinyl)amine (BQAH, 1), (2-pyridin-2-yl-ethyl)-(8-quinolinyl)amine (2-pyridin-2-yl-ethyl-QAH, 2), o-dimethylaminophenyl(8-quinolinyl)amine (o-(NMe2)Ph-QAH, 3), and 3,5-dimethylphenyl(8-quinolinyl)amine (3,5-Me2Ph-QAH, 4) have been prepared in high yield from aryl halide and amine precursors by palladium-catalyzed coupling reactions. Deprotonation of 1 with nBuLi in toluene affords the lithium amide complex [Li][BQA] (5), whose dimeric solid-state crystal structure is presented. Lithium amide 5 was transmetalated by TlOTf to afford the thallium(I) amido complex [Tl][BQA] (6). An X-ray structural study of 6 shows it to be a 1:1 complex of the BQA ligand and Tl. Entry into the group 10 chemistry of the parent ligand 1 was effected by both protolytic and metathetical strategies. Thus, the divalent chloride complexes (BQA)PtCl (7), (BQA)PdCl (8), and (BQA)NiCl (9) were prepared and fully characterized. An X-ray structural study for each of these three complexes shows them to be well-defined, square-planar complexes in which the auxiliary BQA ligand binds in a planar, eta(3)-fashion. For comparison, the reactivity of ligands 2-4 with (COD)PtCl2 was studied. While reaction with ligand 2 afforded an ill-defined product mixture, ligands 3 and 4 reacted with (COD)PtCl2 to generate the unusual alkyl complexes (o-(NMe2)Ph-QA)Pt(1,2-eta(2)-6-sigma-cycloocta-1,4-dienyl) (10) and (3,5-Me2Ph-QA)Pt(1,2-eta(2)-6-sigma-cycloocta-1,4-dienyl) (11), both of which have been structurally characterized.
ABSTRACT
Review what's new in biphasic defibrillation and trauma nursing, including and intubation alternatives.
Subject(s)
Critical Care/trends , Electric Countershock/instrumentation , Electric Countershock/nursing , Intubation, Intratracheal/instrumentation , Intubation, Intratracheal/nursing , Wounds and Injuries/nursing , Critical Care/methods , Electric Countershock/methods , Equipment Design , Humans , Intubation, Intratracheal/methods , Laryngeal MasksABSTRACT
A homoleptic phosphine adduct of thallium(I) supported by a tris(phosphino)borate ligand has been isolated and structurally characterized.
Subject(s)
Catheterization, Peripheral/methods , Catheterization, Peripheral/nursing , Infusions, Intraosseous/methods , Infusions, Intraosseous/nursing , Catheterization, Peripheral/instrumentation , Child , Humans , Infusions, Intraosseous/instrumentation , Patient Selection , Pediatric Nursing/methodsSubject(s)
Bites and Stings/etiology , Bites and Stings/nursing , Emergency Nursing/methods , First Aid/methods , Scyphozoa , Animals , Child , Humans , Male , Nursing Assessment/methodsSubject(s)
Compartment Syndromes/nursing , Nursing Assessment/methods , Adult , Compartment Syndromes/surgery , Emergencies , Female , Humans , LegSubject(s)
Accidents, Traffic , Diaphragm/injuries , Emergency Nursing/methods , Adult , Female , Humans , Nursing Assessment/methods , RuptureABSTRACT
The crystal structure of Ru(2, 2'-bipyridine)2(imidazole)(His83)azurin (RuAz) has been determined to 2.3 A -resolution by X-ray crystallography. The spectroscopic and thermodynamic properties of both the native protein and [Ru(2, 2'-bipyridine)2(imidazole)2]2+ are maintained in the modified protein. Dark-green RuAz crystals grown from PEG 4000, LiNO3, CuCl2 and Tris buffer are monoclinic, belong to the space group C2 and have cell parameters a = 100.6, b = 35.4, c = 74.7 A and beta = 106. 5 degrees. In addition, [Ru(2,2'-bipyridine)2(imidazole)2]SO4 x 10H2O was synthesized, crystallized and structurally characterized by X-ray crystallography. Red-brown crystals of this complex are monoclinic, space group P21/n, unit-cell parameters a = 13.230 (2), b = 18.197 (4), c = 16.126 (4) A, beta = 108.65 (2) degrees. Stereochemical parameters for the refinement of Ru(2, 2'-bipyridine)2(imidazole)(His83) were taken from the atomic coordinates of [Ru(2,2'-bipyridine)2(imidazole)2]2+. The structure of RuAz confirms that His83 is the only site of chemical modification and that the native azurin structure is not perturbed significantly by the ruthenium label.
Subject(s)
Azurin/chemistry , Organometallic Compounds/chemistry , Pseudomonas aeruginosa/chemistry , Ruthenium/chemistry , Crystallography, X-Ray , Electron Spin Resonance Spectroscopy , Magnetic Resonance Spectroscopy , Molecular Structure , Oxidation-Reduction , Protein ConformationABSTRACT
Cytochrome c(2) serves as the secondary electron donor that reduces the photo-oxidized bacteriochlorophyll dimer in photosynthetic bacteria. Cytochrome c(2) from Rhodobacter sphaeroides has been crystallized in three different forms. At high ionic strength, crystals of a hexagonal space group (P6(1)22) were obtained, while at low ionic strength, triclinic (P1) and tetragonal (P4(1)2(1)2) crystals were formed. The three-dimensional structures of the cytochrome in all three crystal forms have been determined by X-ray diffraction at resolutions of 2.20 A (hexagonal), 1.95 A, (triclinic) and 1.53 A (tetragonal). The most significant difference observed was the binding of an imidazole molecule to the iron atom of the heme group in the hexagonal structure. This binding displaces the sulfur atom of Met l00, which forms the axial ligand in the triclinic and tetragonal structures.
ABSTRACT
The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 degrees C, have been determined by X-ray crystallography to a resolution of 1.8 A. Crystals of this rubredoxin grow in space group P2(1)2(1)2(1) with room temperature cell dimensions a = 34.6 A, b = 35.5 A, and c = 44.4 A. Initial phases were determined by the method of molecular replacement using the oxidized form of the rubredoxin from the mesophilic eubacterium, Clostridium pasteurianum, as a starting model. The oxidized and reduced models of P. furiosus rubredoxin each contain 414 nonhydrogen protein atoms comprising 53 residues. The model of the oxidized form contains 61 solvent H2O oxygen atoms and has been refined with X-PLOR and TNT to a final R = 0.178 with root mean square (rms) deviations from ideality in bond distances and bond angles of 0.014 A and 2.06 degrees, respectively. The model of the reduced form contains 37 solvent H2O oxygen atoms and has been refined to R = 0.193 with rms deviations from ideality in bond lengths of 0.012 A and in bond angles of 1.95 degrees. The overall structure of P. furiosus rubredoxin is similar to the structures of mesophilic rubredoxins, with the exception of a more extensive hydrogen-bonding network in the beta-sheet region and multiple electrostatic interactions (salt bridge, hydrogen bonds) of the Glu 14 side chain with groups on three other residues (the amino-terminal nitrogen of Ala 1; the indole nitrogen of Trp 3; and the amide nitrogen group of Phe 29). The influence of these and other features upon the thermostability of the P. furiosus protein is discussed.
Subject(s)
Archaea/metabolism , Protein Conformation , Rubredoxins/chemistry , Amino Acid Sequence , Crystallization , Drug Stability , Hot Temperature , Hydrogen Bonding , Mathematics , Models, Molecular , Molecular Sequence Data , Oxidation-Reduction , Protein Structure, Secondary , Rubredoxins/genetics , Rubredoxins/metabolism , Sequence Homology, Amino Acid , Thermodynamics , X-Ray DiffractionABSTRACT
The three-dimensional X-ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at -161 degrees C, and the NMR structure of the zinc-substituted protein, determined in solution at 45 degrees C, are compared. The NMR and X-ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability.
