Steric and electronic factor comparisons in hydrotris(3-phenylpyrazolyl)borate nickel(II) aryloxides

2016 ◽  
Vol 72 (11) ◽  
pp. 791-796 ◽  
Author(s):  
William L. Green ◽  
Eric R. Sirianni ◽  
Glenn P. A. Yap ◽  
Charles G. Riordan
Keyword(s):  
Metal Ions ◽  
Active Site ◽  
Electronic Factor ◽  
Coordination Site ◽  
Π Stacking ◽  
Alkyl Groups ◽  
Tetrahedral Environment ◽  
Structural Characterizations ◽  
Insight Into

Hydrotris(pyrazolyl)borate (Tp) ligands, also known as scorpionates, are potent tridentate donors that effectively bind metal ions in a face-capping array. Hydrotris(3-phenylpyrazolyl)borate enforces a tetrahedral environment on NiIIto model metalloenzymes. The syntheses and structural characterizations of a number of [hydrotris(3-phenylpyrazolyl)borato]nickel(II) aryloxides were performed to provide insight into the environment of the model active site; these compounds are chlorido[hydrotris(3-phenylpyrazolyl-κN2)borato](3-phenyl-1H-pyrazole-κN2)nickel(II) chloroform monosolvate, [Ni(C27H22BN6)Cl(C9H8N2)]·CHCl3, (2), [hydrotris(3-phenylpyrazolyl-κN2)borato](phenolato-κO)nickel(II), [Ni(C27H22BN6)(C6H5O)], (3), (2,6-dimethylphenolato-κO)[hydrotris(3-phenylpyrazolyl-κN2)borato]nickel(II) [Ni(C27H22BN6)(C8H9O)], (4), (4-tert-butylphenolato-κO)[hydrotris(3-phenylpyrazolyl-κN2)borato]nickel(II), [Ni(C27H22BN6)(C10H13O)], (5), and [hydrotris(3-phenylpyrazolyl-κN2)borato](phenolato-κO)(tetrahydrofuran-κO)nickel(II) tetrahydrofuran monosolvate, [Ni(C27H22BN6)(C6H5O)(C4H8O)]·C4H8O, (6). Alkyl groups,e.g. tert-butyl in (5) and methyl in (4), electronically activate the aryloxide group to intramolecular π–π stacking but can be frustrated by steric encumbrance at the interacting ring faces. The flexibility at the nickel coordination site, afforded by the uncrowded B atom of the TpPhligand, allows tetrahydrofuran coordination in the phenolate compound.

scholarly journals Evaluation of N-Alkyl-bis-o-aminobenzamide Receptors for the Determination and Separation of Metal Ions by Fluorescence, UV-Visible Spectrometry and Zeta Potential

Molecules ◽  
2019 ◽  
Vol 24 (9) ◽  
pp. 1737 ◽  
Author(s):  
Marisela Martinez-Quiroz ◽  
Xiomara E. Aguilar-Martinez ◽  
Mercedes T. Oropeza-Guzman ◽  
Ricardo Valdez ◽  
Eduardo A. Lopez-Maldonado
Keyword(s):  
Aqueous Solution ◽  
Zeta Potential ◽  
Metal Ions ◽  
Environmental Concern ◽  
Separation Of Metal Ions ◽  
Complexing Capacity ◽  
Alkyl Groups ◽  
Molecular Fluorescence ◽  
Uv Visible ◽  
Phase Sensor

This paper presents the synthesis and evaluation of physicochemical behavior of a new series of N-alkyl-bis-o-aminobenzamides (BOABs) in aqueous solution. The study was targeted to the complexing capacity of five metal ions (Fe2+, Cu2+, Cd2+, Hg2+ and Pb2+) of environmental concern as the medullar principle of a liquid phase sensor for its application in the determination of these metal ions due to its versatility of use. Molecular fluorescence, UV-visible and Zeta potential were measured for five BOABs and the effect of alkyl groups with different central chain length (n = 3, 4, 6, 8 and 10) on physicochemical performance determined. The results have shown that these derivatives present higher sensibility and selectivity for Cu2+ even in the presence of the other metal ions. An additional application test was done adding a pectin (0.1 wt %) solution to the BOAB-Cu+2 complex to obtain a precipitate (flocs) as a potential selective separation process of Cu from aqueous solution. The solid was then lyophilized and analyzed by SEM-EDS, the images showed spheric forms containing Cu+2 with diameter of approximately of 8 μm and 30 wt %.

Autophagy and lysosomal dysfunction: A new insight into mechanism of synergistic pulmonary toxicity of carbon black-metal ions co-exposure

Carbon ◽  
2017 ◽  
Vol 111 ◽  
pp. 322-333 ◽  
Author(s):  
Huating Kong ◽  
Kai Xia ◽  
Liang Pan ◽  
Jichao Zhang ◽  
Yan Luo ◽  
...  
Keyword(s):  
Carbon Black ◽  
Metal Ions ◽  
Pulmonary Toxicity ◽  
Black Metal ◽  
Lysosomal Dysfunction ◽  
Insight Into

MetLigDB: a web-based database for the identification of chemical groups to design metalloprotein inhibitors

2011 ◽  
Vol 44 (4) ◽  
pp. 878-881 ◽  
Author(s):  
Hwanho Choi ◽  
Hongsuk Kang ◽  
Hwangseo Park
Keyword(s):  
Drug Discovery ◽  
Metal Ions ◽  
Metal Ion ◽  
Central Metal ◽  
Amino Acid Residues ◽  
Web Based ◽  
Additional Information ◽  
Chemical Groups ◽  
Insight Into ◽  
Chelating Groups

MetLigDB (http://silver.sejong.ac.kr/MetLigDB) is a publicly accessible web-based database through which the interactions between a variety of chelating groups and various central metal ions in the active site of metalloproteins can be explored in detail. Additional information can also be retrieved, including protein and inhibitor names, the amino acid residues coordinated to the central metal ion, and the binding affinity of the inhibitor for the target metalloprotein. Although many metalloproteins have been considered promising targets for drug discovery, it is difficult to discover new inhibitors because of the difficulty in designing a suitable chelating moiety to impair the catalytic activity of the central metal ion. Because both common and specific chelating groups can be identified for varying metal ions and the associated coordination environments, MetLigDB is expected to give users insight into designing new inhibitors of metalloproteins for drug discovery.

X-ray photoemission studies of the interaction of metals and metal ions with DNA

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Esha Mishra ◽  
Subrata Majumder ◽  
Shikha Varma ◽  
Peter A. Dowben
Keyword(s):  
Heavy Metal ◽  
Metal Ions ◽  
Conformational Changes ◽  
Photoelectron Spectroscopy ◽  
X Ray ◽  
Surface Sensitivity ◽  
Metal Interaction ◽  
The Status ◽  
Sensitivity And Selectivity ◽  
Insight Into

Abstract X-ray Photoelectron Spectroscopy (XPS) has been used to study the interactions of heavy metal ions with DNA with some success. Surface sensitivity and selectivity of XPS are advantageous for identifying and characterizing the chemical and elemental structure of the DNA to metal interaction. This review summarizes the status of what amounts to a large part of the photoemission investigations of biomolecule interactions with metals and offers insight into the mechanism for heavy metal-bio interface interactions. Specifically, it is seen that metal interaction with DNA results in conformational changes in the DNA structure.

The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities

2014 ◽  
Vol 70 (12) ◽  
pp. 3212-3225 ◽  
Author(s):  
Tiila-Riikka Kiema ◽  
Rajesh K. Harijan ◽  
Malgorzata Strozyk ◽  
Toshiyuki Fukao ◽  
Stefan E. H. Alexson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Reaction Mechanism ◽  
Active Site ◽  
Quaternary Structure ◽  
Fatty Acyl ◽  
Physiological Importance ◽  
Loop Domain ◽  
Solution Studies ◽  
Hydrolysis Of ◽  
Insight Into

Crystal structures of human mitochondrial 3-ketoacyl-CoA thiolase (hT1) in the apo form and in complex with CoA have been determined at 2.0 Å resolution. The structures confirm the tetrameric quaternary structure of this degradative thiolase. The active site is surprisingly similar to the active site of theZoogloea ramigerabiosynthetic tetrameric thiolase (PDB entries 1dm3 and 1m1o) and different from the active site of the peroxisomal dimeric degradative thiolase (PDB entries 1afw and 2iik). A cavity analysis suggests a mode of binding for the fatty-acyl tail in a tunnel lined by the Nβ2–Nα2 loop of the adjacent subunit and the Lα1 helix of the loop domain. Soaking of the apo hT1 crystals with octanoyl-CoA resulted in a crystal structure in complex with CoA owing to the intrinsic acyl-CoA thioesterase activity of hT1. Solution studies confirm that hT1 has low acyl-CoA thioesterase activity for fatty acyl-CoA substrates. The fastest rate is observed for the hydrolysis of butyryl-CoA. It is also shown that T1 has significant biosynthetic thiolase activity, which is predicted to be of physiological importance.

Sign in / Sign up

Export Citation Format

Share Document