Comparison of the Extent of Macrochelate Formation in Complexes of Divalent Metal Ions with Guanosine (GMP2-), Inosine (IMP2-), and Adenosine 5'-Monophosphate (AMP2-). The Crucial Role of N-7 Basicity in Metal Ion-Nucleic Base Recognition

1994 ◽  
Vol 116 (7) ◽  
pp. 2958-2971 ◽  
Author(s):  
Helmut Sigel ◽  
Salah S. Massoud ◽  
Nicolas A. Corfu
Keyword(s):  
Metal Ions ◽  
Crucial Role ◽  
Metal Ion ◽  
Divalent Metal ◽  
Divalent Metal Ions

scholarly journals The Crucial Role of Divalent Metal Ions in the DNA-Acting Efficacy and Inhibition of the Transcription of Dimeric Chromomycin A3

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e43792 ◽  
Author(s):  
Chun-Wei Hsu ◽  
Show-Mei Chuang ◽  
Wen-Ling Wu ◽  
Ming-Hon Hou
Keyword(s):  
Metal Ions ◽  
Crucial Role ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Chromomycin A3

scholarly journals Rhizosphere Acidification by Iron Deficient Bean Plants: The Role of Trace Amounts of Divalent Metal Ions

1989 ◽  
Vol 90 (1) ◽  
pp. 359-364 ◽  
Author(s):  
H. Frits Bienfait ◽  
Henk J. Lubberding ◽  
Peter Heutink ◽  
L. Lindner ◽  
Jacques Visser ◽  
...  
Keyword(s):  
Metal Ions ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Rhizosphere Acidification ◽  
Bean Plants ◽  
Iron Deficient

scholarly journals A dual role of divalent metal ions in catalysis and folding of RNase H1 from extreme halophilic archaeonHalobacteriumsp. NRC-1

FEBS Open Bio ◽  
2012 ◽  
Vol 2 (1) ◽  
pp. 345-352 ◽  
Author(s):  
Elias Tannous ◽  
Koji Yokoyama ◽  
Dong-Ju You ◽  
Yuichi Koga ◽  
Shigenori Kanaya
Keyword(s):  
Metal Ions ◽  
Divalent Metal ◽  
Dual Role ◽  
Divalent Metal Ions

Role of divalent metal ions in the hammerhead RNA cleavage reaction

Biochemistry ◽  
1991 ◽  
Vol 30 (39) ◽  
pp. 9464-9469 ◽  
Author(s):  
SueAnn C. Dahm ◽  
Olke C. Uhlenbeck
Keyword(s):  
Metal Ions ◽  
Divalent Metal ◽  
Rna Cleavage ◽  
Divalent Metal Ions ◽  
Cleavage Reaction ◽  
Hammerhead Rna

scholarly journals Structure of New Binary and Ternary DNA Polymerase Complexes From Bacteriophage RB69

2021 ◽  
Vol 8 ◽  
Author(s):  
Jongseo Park ◽  
Hyung-Seop Youn ◽  
Jun Yop An ◽  
Youngjin Lee ◽  
Soo Hyun Eom ◽  
...  
Keyword(s):  
Metal Ions ◽  
Dna Polymerase ◽  
Metal Ion ◽  
Ternary Complex ◽  
Critical Role ◽  
Divalent Metal ◽  
Binary Complex ◽  
Divalent Metal Ions ◽  
Divalent Metal Ion ◽  
Initial Binding

DNA polymerase plays a critical role in passing the genetic information of any living organism to its offspring. DNA polymerase from enterobacteria phage RB69 (RB69pol) has both polymerization and exonuclease activities and has been extensively studied as a model system for B-family DNA polymerases. Many binary and ternary complex structures of RB69pol are known, and they all contain a single polymerase-primer/template (P/T) DNA complex. Here, we report a crystal structure of the exonuclease-deficient RB69pol with the P/T duplex in a dimeric form at a resolution of 2.2 Å. The structure includes one new closed ternary complex with a single divalent metal ion bound and one new open binary complex in the pre-insertion state with a vacant dNTP-binding pocket. These complexes suggest that initial binding of the correct dNTP in the open state is much weaker than expected and that initial binding of the second divalent metal ion in the closed state is also much weaker than measured. Additional conformational changes are required to convert these complexes to high-affinity states. Thus, the measured affinities for the correct incoming dNTP and divalent metal ions are average values from many conformationally distinctive states. Our structure provides new insights into the order of the complex assembly involving two divalent metal ions. The biological relevance of specific interactions observed between one RB69pol and the P/T duplex bound to the second RB69pol observed within this dimeric complex is discussed.

scholarly journals Modeling of neotame and fructose thermochemistry: Comparison with mono and divalent metal ions by Computational and experimental approach

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Deepali Sharma ◽  
Suvardhan Kanchi ◽  
Ayyappa Bathinapatla ◽  
Inamuddin ◽  
Abdullah M. Asiri
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Density Functional ◽  
Divalent Metal ◽  
Basis Set ◽  
Hydroxyl Groups ◽  
Specific Cell ◽  
Water Medium ◽  
Artificial Sweetener ◽  
Divalent Metal Ions

AbstractThe metal complexes can demonstrate various interesting biological activities in the human body. However, the role of certain metal ions for specific cell activities is still subject to debate. This study is aimed at comparing the thermochemical properties of neotame (artificial sweetener) and α, β-fructose in gas phase and water medium. The interaction of α and β-fructose, neotame with monovalent and divalent metal ions was studied and comprehended by density functional theory (DFT) using B3LYP functional, 6–311 + G (d, p) and D3 basis set. Metal ion affinities (MIA) values depicted that ionic radius of metal ions played an important role in the interaction of α, β-fructose and neotame. The ∆G parameter was calculated to predict and understand the interaction of metal ions with α and β-fructose, neotame. The results suggested that the presence of hydroxyl groups and oxygen atoms in sugar molecules acted as preferred sites for the binding and interaction of mono and divalent ions. For the first time computational study has been introduced in the present study to review the progress in the application of metal binding with sugar molecules especially with neotame. Moreover, voltammetric behaviour of neotame-Zn2+ was studied using cyclic and differential pulse voltammetry. The obtained results suggest that the peak at −1.13 V is due to the reduction of Zn2+ in 0.1 M phosphate buffer medium at pH 5.5. Whereas, addition of 6-fold higher concentration of neotame to the ZnCl2.2H2O resulted in a new irreversible cathodic peak at −0.83, due to the reduction of neotame-Zn2+ complex. The Fourier transform infrared spectroscopy (FTIR) results indicates that the β-amino group (-NH) and carboxyl carbonyl (-C = O) groups of neotame is participating in the chelation process, which is further supported by DFT studies. The findings of this study identify the efficient chelation factors as major contributors into metal ion affinities, with promising possibilities to determine important biological processes in cell wall and glucose transmembrane transport.

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