Metal ion concentration, time, and pH dependence of metal ion binding to a transferrin metalloprotein affinity chromatography (MAMC) matrix

1995 ◽  
Vol 64 (1) ◽  
pp. 96-100 ◽  
Author(s):  
Kevin P. Cannell ◽  
John B. Vincent
Keyword(s):  
Affinity Chromatography ◽  
Metal Ion ◽  
Ph Dependence ◽  
Ion Concentration ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Concentration Time

The pH dependence of metal ion binding to the native zinc site of bovine erythrocuprein (superoxide dismutase)

1982 ◽  
Vol 104 (6) ◽  
pp. 1717-1723 ◽  
Author(s):  
Michael W. Pantoliano ◽  
Joan S. Valentine ◽  
Robert J. Mammone ◽  
Diane M. Scholler
Keyword(s):  
Superoxide Dismutase ◽  
Metal Ion ◽  
Ph Dependence ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Zinc Site

METAL ION BINDING BY ALGAE AND HIGHER PLANT TISSUES: A Phenomenological Study of Solution pH Dependence

1994 ◽  
Vol 12 (4) ◽  
pp. 803-816 ◽  
Author(s):  
Jesus R. Lujan ◽  
Dennis W. Darnall ◽  
Peter C. Stark ◽  
Gary D. Rayson ◽  
Jorge L. Gardea-Torresdey
Keyword(s):  
Metal Ion ◽  
Phenomenological Study ◽  
Ph Dependence ◽  
Plant Tissues ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Solution Ph ◽  
Higher Plant

Circularly polarized luminiscence as a probe of metal ions binding sites in calmodulin

1991 ◽  
Vol 56 (12) ◽  
pp. 3028-3031 ◽  
Author(s):  
Nursen Coruh ◽  
James P. Riehl
Keyword(s):  
Metal Ions ◽  
Binding Sites ◽  
Metal Ion ◽  
Ion Concentration ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Circularly Polarized ◽  
Ion Binding Sites ◽  
Metal Ion Binding Sites ◽  
Dissymmetry Ratio

Circularly polarized luminiscence (CPL) from dilute solutions of Tb(III) bound to the Ca-binding protein calmodulin is reported. The dissymmetry ratio, gem, at 543.5 nm can be monitored as a function of equivalents of metal ion concentration. Competitive and consecutive addition of Ca(II) versus Tb(III) yield results which are consistent with previous results that suggest that Tb(III) and Ca(II) have a preferred affinity for different metal-ion binding sites in this protein.

Photophysical Characterisation, Metal Ion Binding and Enantiomeric Recognition of Chiral Ligands Containing Phenazine Fluorophore

2004 ◽  
Vol 69 (4) ◽  
pp. 885-896 ◽  
Author(s):  
Luisa Stella Dolci ◽  
Péter Huszthy ◽  
Erika Samu ◽  
Marco Montalti ◽  
Luca Prodi ◽  
...  
Keyword(s):  
Metal Ion ◽  
Photophysical Properties ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ammonium Ions ◽  
Enantiomerically Pure ◽  
Binding Process ◽  
High Affinity ◽  
Enantiomeric Recognition ◽  
Chiral Species

Enantiomerically pure dimethyl- and diisobutyl-substituted phenazino-18-crown-6 ligands bind metal and ammonium ions and also primary aralkylammonium perchlorates in acetonitrile with high affinity, causing pronounced changes in their luminescence properties. In addition, they show enantioselectivity towards chiral primary aralkylammonium perchlorates. The possibility to monitor the binding process by photoluminescence spectroscopy can gain ground for the design of very efficient enantioselective chemosensors for chiral species. The observed changes in the photophysical properties are also an important tool for understanding the interactions present in the adduct.

scholarly journals Snapshots of a Non-Canonical RdRP in Action

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1260
Author(s):  
Diego S. Ferrero ◽  
Michela Falqui ◽  
Nuria Verdaguer
Keyword(s):  
Metal Ion ◽  
Rna Viruses ◽  
Ion Binding ◽  
Genome Replication ◽  
Metal Ion Binding ◽  
Insect Virus ◽  
X Ray ◽  
Template Strand ◽  
Nucleotide Incorporation ◽  
Elongation Process

RNA viruses typically encode their own RNA-dependent RNA polymerase (RdRP) to ensure genome replication and transcription. The closed “right hand” architecture of RdRPs encircles seven conserved structural motifs (A to G) that regulate the polymerization activity. The four palm motifs, arranged in the sequential order A to D, are common to all known template dependent polynucleotide polymerases, with motifs A and C containing the catalytic aspartic acid residues. Exceptions to this design have been reported in members of the Permutotetraviridae and Birnaviridae families of positive single stranded (+ss) and double-stranded (ds) RNA viruses, respectively. In these enzymes, motif C is located upstream of motif A, displaying a permuted C–A–B–D connectivity. Here we study the details of the replication elongation process in the non-canonical RdRP of the Thosea asigna virus (TaV), an insect virus from the Permutatetraviridae family. We report the X-ray structures of three replicative complexes of the TaV polymerase obtained with an RNA template-primer in the absence and in the presence of incoming rNTPs. The structures captured different replication events and allowed to define the critical interactions involved in: (i) the positioning of the acceptor base of the template strand, (ii) the positioning of the 3’-OH group of the primer nucleotide during RNA replication and (iii) the recognition and positioning of the incoming nucleotide. Structural comparisons unveiled a closure of the active site on the RNA template-primer binding, before rNTP entry. This conformational rearrangement that also includes the repositioning of the motif A aspartate for the catalytic reaction to take place is maintained on rNTP and metal ion binding and after nucleotide incorporation, before translocation.

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