scholarly journals Chemistry and Some Biological Potential of Bismuth and Antimony Dithiocarbamate Complexes

Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 305 ◽  
Author(s):  
Jerry O. Adeyemi ◽  
Damian C. Onwudiwe
Keyword(s):  
Solid State ◽  
Binding Sites ◽  
Metal Ion ◽  
Antifungal Agents ◽  
Biological Function ◽  
Structural Diversity ◽  
Supramolecular Assemblies ◽  
Materials Chemistry ◽  
Interesting Application ◽  
Biological Potential

Interest in the synthesis of Bi(III) and Sb(III) dithiocarbamate complexes is on the rise, and this has been attributed to their wide structural diversity and their interesting application as biological agents and in solid state/materials chemistry. The readily available binding sites of the two sulphur atoms within the dithiocarbamate moiety in the complexes confers a wide variety of geometry and interactions that often leads to supramolecular assemblies. Although none of the bismuth or antimony metals are known to play any natural biological function, their dithiocarbamate complexes, however, have proven very useful as antibacterial, antileishmanial, anticancer, and antifungal agents. The dithiocarbamate ligands modulate the associated toxicity of the metals, especially antimony, since bismuth is known to be benign, allowing the metal ion to get to the targeted sites; hence, making it less available for side and other damaging reactions. This review presents a concise chemistry and some known biological potentials of their trivalent dithiocarbamate complexes.

scholarly journals Characterization of the two 5-aminolaevulinic acid binding sites, the A- and P-sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli

1995 ◽  
Vol 305 (1) ◽  
pp. 151-158 ◽  
Author(s):  
P Spencer ◽  
P M Jordan
Keyword(s):  
Schiff Base ◽  
Binding Sites ◽  
Metal Ion ◽  
Substrate Binding ◽  
Aminolaevulinic Acid ◽  
Acid Dehydratase ◽  
Carboxylate Groups ◽  
Catalytic Metal ◽  
A Site ◽  
Aminolaevulinic Acid Dehydratase

Experiments are described in which the individual properties of the two 5-aminolaevulinic acid (ALA) binding sites, the A-site and the P-site, of 5-aminolaevulinic acid dehydratase (ALAD) have been investigated. The ALA binding affinity at the A-site is greatly enhanced (at least 10-fold) on the binding of the catalytic metal ion (bound at the alpha-site). The nature of the catalytic metal ion, Mg2+ or Zn2+, also gave major variations in the substrate Km, P-site affinity for ALA, the effect of potassium and phosphate ions and the pH-dependence of substrate binding. Modification of the P-site by reaction of the enzyme-substrate Schiff base with NaBH4 and analysis of the reduced adduct by electro-spray mass spectrometry indicated a maximum of 1 mol of substrate incorporated/mol of subunit, correlating with a linear loss of enzyme activity. The reduced Schiff-base adduct was used to investigate substrate binding at the A-site by using rate-of-dialysis analysis. The affinity for ALA at the A-site of Mg alpha Zn beta ALAD was found to determine the Km for the reaction and was pH-dependent, with its affinity increasing from 1 mM at pH 6 to 70 microM at pH 8.5. The affinity of ALA at the P-site of Zn alpha An beta ALAD is proposed to limit the Km at pH values above 7, since the measured Kd for ALA at the A-site in 45 microM Tris, pH 8, was well below the observed Km (600 microM) under the same conditions. The amino group of the ALA molecule bound at the P-site was identified as a critical binding component for the A-site, explaining why ALA binding to ALAD is ordered, with the P-site ALA binding first. Structural requirements for ALA binding at the A- and P-sites have been identified: the P-site requires the carbonyl and carboxylate groups, whereas the A-site requires the amino, carbonyl and carboxylate groups of the substrate.

The influence of metal-ion binding on the structure and surface composition of Sonic Hedgehog: a combined classical and hybrid QM/MM MD study

2016 ◽  
Vol 18 (32) ◽  
pp. 22254-22265 ◽  
Author(s):  
Manuel Hitzenberger ◽  
Thomas S. Hofer
Keyword(s):  
Metal Ions ◽  
Sonic Hedgehog ◽  
Binding Sites ◽  
Metal Ion ◽  
Surface Composition ◽  
Quantum Mechanical ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Structural Impact

The interaction of metal ions with Shh binding-sites and their structural impact are assessed via classical and quantum mechanical simulations.

scholarly journals Lignocellulose Affects Mn2+ Regulation of Peroxidase Transcript Levels in Solid-State Cultures of Pleurotus ostreatus

2002 ◽  
Vol 68 (6) ◽  
pp. 3156-3158 ◽  
Author(s):  
Roni Cohen ◽  
Oded Yarden ◽  
Yitzhak Hadar
Keyword(s):  
Gene Expression ◽  
Solid State ◽  
Direct Effect ◽  
Pleurotus Ostreatus ◽  
Metal Ion ◽  
Transcript Levels ◽  
Peroxidase Gene ◽  
Defined Media ◽  
Cotton Stalks ◽  
Encoding Genes

ABSTRACT The effect of Mn2+ amendment on peroxidase gene expression was studied during Pleurotus ostreatus growth on cotton stalks. Four peroxidase-encoding genes were expressed differentially and in a manner different from that observed in defined media. Mn2+ affects mnp3 expression even 2 h after its addition to the cultures, suggesting a direct effect of the metal ion on expression.

scholarly journals Selective Inhibition of DNA Replicase Assembly by a Non-natural Nucleotide: Exploiting the Structural Diversity of ATP-Binding Sites

2009 ◽  
Vol 5 (2) ◽  
pp. 183-194 ◽  
Author(s):  
Kevin Eng ◽  
Sarah K. Scouten-Ponticelli ◽  
Mark Sutton ◽  
Anthony Berdis
Keyword(s):  
Binding Sites ◽  
Structural Diversity ◽  
Selective Inhibition ◽  
Atp Binding ◽  
Dna Replicase

scholarly journals Chemical Diversity and Biological Activity of Secondary Metabolites Isolated from Indonesian Marine Invertebrates

Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 1898
Author(s):  
Fauzia Izzati ◽  
Mega Ferdina Warsito ◽  
Asep Bayu ◽  
Anggia Prasetyoputri ◽  
Akhirta Atikana ◽  
...  
Keyword(s):  
Natural Products ◽  
Bioactive Compounds ◽  
Marine Natural Products ◽  
Biological Function ◽  
Marine Invertebrates ◽  
Biological Activities ◽  
Structural Diversity ◽  
Chemical Diversity ◽  
Soft Corals ◽  
High Chemical

Marine invertebrates have been reported to be an excellent resource of many novel bioactive compounds. Studies reported that Indonesia has remarkable yet underexplored marine natural products, with a high chemical diversity and a broad spectrum of biological activities. This review discusses recent updates on the exploration of marine natural products from Indonesian marine invertebrates (i.e., sponges, tunicates, and soft corals) throughout 2007–2020. This paper summarizes the structural diversity and biological function of the bioactive compounds isolated from Indonesian marine invertebrates as antimicrobial, antifungal, anticancer, and antiviral, while also presenting the opportunity for further investigation of novel compounds derived from Indonesian marine invertebrates.

Structural diversity of new solid-state luminophores based on quinoxaline-β-ketoiminate boron difluoride complexes with remarkable fluorescence switching properties

2015 ◽  
Vol 51 (13) ◽  
pp. 2656-2659 ◽  
Author(s):  
Chia-Wei Liao ◽  
Rajeswara Rao M. ◽  
Shih-Sheng Sun
Keyword(s):  
Solid State ◽  
Structural Diversity ◽  
Acid Base ◽  
Fluorescence Switching ◽  
Solid State Fluorescence ◽  
Boron Difluoride

Highly tunable organoboron luminophores with intense solid-state fluorescence showed outstanding photoswitching properties modulated by acid/base vapors.

Copper(II) and zinc(II) dinuclear enzymes model compounds: The nature of the metal ion in the biological function

2017 ◽  
Vol 1150 ◽  
pp. 316-328 ◽  
Author(s):  
L.G. Ferraresso ◽  
E.G.R. de Arruda ◽  
T.P.L. de Moraes ◽  
R.B. Fazzi ◽  
A.M. Da Costa Ferreira ◽  
...  
Keyword(s):  
Metal Ion ◽  
Biological Function ◽  
Model Compounds
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