Stability and thermodynamics of ligand‐free tin–gold clusters

1986 ◽  
Vol 84 (6) ◽  
pp. 3432-3438 ◽  
Author(s):  
J. E. Kingcade ◽  
K. A. Gingerich
Keyword(s):  
Gold Clusters ◽  
Ligand Free

Stability of ligand free tin-gold clusters

1975 ◽  
Vol 14 ◽  
pp. L47-L48 ◽  
Author(s):  
K.A. Gingerich ◽  
D.L. Cocke ◽  
U.V. Choudary
Keyword(s):  
Gold Clusters ◽  
Ligand Free

Stability and thermodynamics of ligand-free germanium-gold clusters

1979 ◽  
Vol 18 (11) ◽  
pp. 3094-3104 ◽  
Author(s):  
J. E. Kingcade ◽  
U. V. Choudary ◽  
K. A. Gingerich
Keyword(s):  
Gold Clusters ◽  
Ligand Free ◽  
Germanium Gold

ChemInform Abstract: STABILITY AND THERMODYNAMICS OF LIGAND-FREE GERMANIUM-GOLD CLUSTERS

1980 ◽  
Vol 11 (10) ◽  
Author(s):  
J. E. JUN. KINGCADE ◽  
U. V. CHOUDARY ◽  
K. A. GINGERICH
Keyword(s):  
Gold Clusters ◽  
Ligand Free ◽  
Germanium Gold

Crystal structure images of large gold clusters and growing crystals by HRTEM

1984 ◽  
Vol 42 ◽  
pp. 428-429
Author(s):  
L.R. Wallenberg ◽  
J.-O. Bovin ◽  
G. Schmid
Keyword(s):  
Crystal Structure ◽  
Nucleation And Growth ◽  
Close Packing ◽  
Gold Clusters ◽  
Molecular Weight Determination ◽  
Growth Mechanisms ◽  
Starting Point ◽  
Different Types ◽  
Nucleation And Growth Mechanisms ◽  
Points Of View

Metallic clusters are interesting from various points of view, e.g. as a mean of spreading expensive catalysts on a support, or following heterogeneous and homogeneous catalytic events. It is also possible to study nucleation and growth mechanisms for crystals with the cluster as known starting point.Gold-clusters containing 55 atoms were manufactured by reducing (C6H5)3PAuCl with B2H6 in benzene. The chemical composition was found to be Au9.2[P(C6H5)3]2Cl. Molecular-weight determination by means of an ultracentrifuge gave the formula Au55[P(C6H5)3]Cl6 A model was proposed from Mössbauer spectra by Schmid et al. with cubic close-packing of the 55 gold atoms in a cubeoctahedron as shown in Fig 1. The cluster is almost completely isolated from the surroundings by the twelve triphenylphosphane groups situated in each corner, and the chlorine atoms on the centre of the 3x3 square surfaces. This gives four groups of gold atoms, depending on the different types of surrounding.

Aldehyde gold clusters for molecular labeling

1995 ◽  
Vol 53 ◽  
pp. 858-859
Author(s):  
James F. Hainfeld ◽  
Frederic R. Furuya
Keyword(s):  
Covalent Bond ◽  
Aldehyde Group ◽  
Gold Clusters ◽  
Side Reactions ◽  
Amino Groups ◽  
Sodium Cyanoborohydride ◽  
Schiff’S Base ◽  
Protein Molecules ◽  
Hydroxysuccinimide Esters ◽  
Primary Amino

Glutaraldehyde is a useful tissue and molecular fixing reagents. The aldehyde moiety reacts mainly with primary amino groups to form a Schiff's base, which is reversible but reasonably stable at pH 7; a stable covalent bond may be formed by reduction with, e.g., sodium cyanoborohydride (Fig. 1). The bifunctional glutaraldehyde, (CHO-(CH2)3-CHO), successfully stabilizes protein molecules due to generally plentiful amines on their surface; bovine serum albumin has 60; 59 lysines + 1 α-amino. With some enzymes, catalytic activity after fixing is preserved; with respect to antigens, glutaraldehyde treatment can compromise their recognition by antibodies in some cases. Complicating the chemistry somewhat are the reported side reactions, where glutaraldehyde reacts with other amino acid side chains, cysteine, histidine, and tyrosine. It has also been reported that glutaraldehyde can polymerize in aqueous solution. Newer crosslinkers have been found that are more specific for the amino group, such as the N-hydroxysuccinimide esters, and are commonly preferred for forming conjugates. However, most of these linkers hydrolyze in solution, so that the activity is lost over several hours, whereas the aldehyde group is stable in solution, and may have an advantage of overall efficiency.

CarR, a MarR-family regulator from Corynebacterium glutamicum, modulated antibiotic and aromatic compound resistance

2019 ◽  
Vol 476 (21) ◽  
pp. 3141-3159 ◽  
Author(s):  
Meiru Si ◽  
Can Chen ◽  
Zengfan Wei ◽  
Zhijin Gong ◽  
GuiZhi Li ◽  
...  
Keyword(s):  
Stress Response ◽  
Ligand Binding ◽  
Corynebacterium Glutamicum ◽  
Conformational Changes ◽  
Cysteine Oxidation ◽  
Transcriptional Regulatory ◽  
Ligand Free ◽  
Redox Sensing

Abstract MarR (multiple antibiotic resistance regulator) proteins are a family of transcriptional regulators that is prevalent in Corynebacterium glutamicum. Understanding the physiological and biochemical function of MarR homologs in C. glutamicum has focused on cysteine oxidation-based redox-sensing and substrate metabolism-involving regulators. In this study, we characterized the stress-related ligand-binding functions of the C. glutamicum MarR-type regulator CarR (C. glutamicum antibiotic-responding regulator). We demonstrate that CarR negatively regulates the expression of the carR (ncgl2886)–uspA (ncgl2887) operon and the adjacent, oppositely oriented gene ncgl2885, encoding the hypothetical deacylase DecE. We also show that CarR directly activates transcription of the ncgl2882–ncgl2884 operon, encoding the peptidoglycan synthesis operon (PSO) located upstream of carR in the opposite orientation. The addition of stress-associated ligands such as penicillin and streptomycin induced carR, uspA, decE, and PSO expression in vivo, as well as attenuated binding of CarR to operator DNA in vitro. Importantly, stress response-induced up-regulation of carR, uspA, and PSO gene expression correlated with cell resistance to β-lactam antibiotics and aromatic compounds. Six highly conserved residues in CarR were found to strongly influence its ligand binding and transcriptional regulatory properties. Collectively, the results indicate that the ligand binding of CarR induces its dissociation from the carR–uspA promoter to derepress carR and uspA transcription. Ligand-free CarR also activates PSO expression, which in turn contributes to C. glutamicum stress resistance. The outcomes indicate that the stress response mechanism of CarR in C. glutamicum occurs via ligand-induced conformational changes to the protein, not via cysteine oxidation-based thiol modifications.

Copper-Catalyzed Hydrocarboxylation of Allenes

2019 ◽  
Author(s):  
Rémi blieck ◽  
Marc Taillefer ◽  
Florian Monnier
Keyword(s):  
Carboxylic Acids ◽  
Copper Catalysis ◽  
Ligand Free ◽  
First Time

The addition of carboxylic acids to allenes was performed for the first time with copper catalysis. The hydrocarboxylation reaction is totally regio- and stereoselective, ligand-free and used catalytic amounts of copper and base.

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