Catalytic mechanism of Na on coal pyrolysis-derived carbon black formation: Experiment and DFT simulation

In the previous paper, the author reported on a technique for preparing vapor-deposited single crystal films as high resolution standards for electron microscopy. The present paper is intended to describe the preparation of several high resolution standards for dark field microscopy and also to mention some results obtained from these studies. Three preparations were used initially: 1.) Graphitized carbon black, 2.) Epitaxially grown particles of different metals prepared by vapor deposition, and 3.) Particles grown epitaxially on the edge of micro-holes formed in a gold single crystal film.The authors successfully obtained dark field micrographs demonstrating the 3.4Å lattice spacing of graphitized carbon black and the Au single crystal (111) lattice of 2.35Å. The latter spacing is especially suitable for dark field imaging because of its preparation, as in 3.), above. After the deposited film of Au (001) orientation is prepared at 400°C the substrate temperature is raised, resulting in the formation of many square micro-holes caused by partial evaporation of the Au film.

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Extraction and identification of fillers and pigments from pyrolyzed rubber and tire samples

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100163332 ◽

1996 ◽

Vol 54 ◽

pp. 174-175

Author(s):

P. Sadhukhan ◽

J. B. Zimmerman

Keyword(s):

Zinc Oxide ◽

Electron Microscope ◽

Carbon Black ◽

Natural Rubber ◽

Transmission Electron Microscope ◽

Rolling Resistance ◽

Synthetic Polymers ◽

Nitrogen Atmosphere ◽

Transmission Electron ◽

Curing Agents

Rubber stocks, specially tires, are composed of natural rubber and synthetic polymers and also of several compounding ingredients, such as carbon black, silica, zinc oxide etc. These are generally mixed and vulcanized with additional curing agents, mainly organic in nature, to achieve certain “designing properties” including wear, traction, rolling resistance and handling of tires. Considerable importance is, therefore, attached both by the manufacturers and their competitors to be able to extract, identify and characterize various types of fillers and pigments. Several analytical procedures have been in use to extract, preferentially, these fillers and pigments and subsequently identify and characterize them under a transmission electron microscope.Rubber stocks and tire sections are subjected to heat under nitrogen atmosphere to 550°C for one hour and then cooled under nitrogen to remove polymers, leaving behind carbon black, silica and zinc oxide and 650°C to eliminate carbon blacks, leaving only silica and zinc oxide.

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Structures of c-di-GMP/cGAMP degrading phosphodiesterase VcEAL: identification of a novel conformational switch and its implication

Biochemical Journal ◽

10.1042/bcj20190399 ◽

2019 ◽

Vol 476 (21) ◽

pp. 3333-3353 ◽

Cited By ~ 3

Author(s):

Malti Yadav ◽

Kamalendu Pal ◽

Udayaditya Sen

Keyword(s):

Active Site ◽

Metal Binding ◽

Metal Ion ◽

Triosephosphate Isomerase ◽

Catalytic Mechanism ◽

Degradation Mechanism ◽

Structural Basis ◽

Conserved Residues ◽

Phosphodiester Bond ◽

Cyclic Dinucleotides

Cyclic dinucleotides (CDNs) have emerged as the central molecules that aid bacteria to adapt and thrive in changing environmental conditions. Therefore, tight regulation of intracellular CDN concentration by counteracting the action of dinucleotide cyclases and phosphodiesterases (PDEs) is critical. Here, we demonstrate that a putative stand-alone EAL domain PDE from Vibrio cholerae (VcEAL) is capable to degrade both the second messenger c-di-GMP and hybrid 3′3′-cyclic GMP–AMP (cGAMP). To unveil their degradation mechanism, we have determined high-resolution crystal structures of VcEAL with Ca2+, c-di-GMP-Ca2+, 5′-pGpG-Ca2+ and cGAMP-Ca2+, the latter provides the first structural basis of cGAMP hydrolysis. Structural studies reveal a typical triosephosphate isomerase barrel-fold with substrate c-di-GMP/cGAMP bound in an extended conformation. Highly conserved residues specifically bind the guanine base of c-di-GMP/cGAMP in the G2 site while the semi-conserved nature of residues at the G1 site could act as a specificity determinant. Two metal ions, co-ordinated with six stubbornly conserved residues and two non-bridging scissile phosphate oxygens of c-di-GMP/cGAMP, activate a water molecule for an in-line attack on the phosphodiester bond, supporting two-metal ion-based catalytic mechanism. PDE activity and biofilm assays of several prudently designed mutants collectively demonstrate that VcEAL active site is charge and size optimized. Intriguingly, in VcEAL-5′-pGpG-Ca2+ structure, β5–α5 loop adopts a novel conformation that along with conserved E131 creates a new metal-binding site. This novel conformation along with several subtle changes in the active site designate VcEAL-5′-pGpG-Ca2+ structure quite different from other 5′-pGpG bound structures reported earlier.

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