scholarly journals Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy

2017 ◽  
Vol 2017 ◽  
pp. 1-7 ◽  
Author(s):  
Valeria Sivo ◽  
Gianluca D’Abrosca ◽  
Luigi Russo ◽  
Rosa Iacovino ◽  
Paolo Vincenzo Pedone ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Coordination Sphere ◽  
Metal Ion ◽  
Electronic Configuration ◽  
Transition Band ◽  
Tetrahedral Geometry ◽  
Vis Spectroscopy ◽  
Zinc Finger Domains ◽  
Spectroscopic Probe

Co(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Here, exploiting the capability of the prokaryotic zinc finger to use different combinations of residues to properly coordinate the structural metal ion, we provide the UV-Vis characterization of Co(II) addition to Ros87 and its mutant Ros87_C27D which bears an unusual CysAspHis2 coordination sphere. Zinc finger sites containing only one cysteine have been infrequently characterized. We show for the CysAspHis2 coordination an intense d-d transition band, blue-shifted with respect to the Cys2His2 sphere. These data complemented by NMR and CD data demonstrate that the tetrahedral geometry of the metal site is retained also in the case of a single-cysteine coordination sphere.

scholarly journals The structural role of the zinc ion can be dispensable in prokaryotic zinc-finger domains

2009 ◽  
Vol 106 (17) ◽  
pp. 6933-6938 ◽  
Author(s):  
Ilaria Baglivo ◽  
Luigi Russo ◽  
Sabrina Esposito ◽  
Gaetano Malgieri ◽  
Mario Renda ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Coordination Sphere ◽  
Zinc Ion ◽  
Binding Domain ◽  
Hydrophobic Core ◽  
Zinc Finger Domain ◽  
High Sequence Identity ◽  
Zinc Coordination ◽  
Zinc Finger Domains

The recent characterization of the prokaryotic Cys2His2 zinc-finger domain, identified in Ros protein from Agrobacterium tumefaciens, has demonstrated that, although possessing a similar zinc coordination sphere, this domain is structurally very different from its eukaryotic counterpart. A search in the databases has identified ≈300 homologues with a high sequence identity to the Ros protein, including the amino acids that form the extensive hydrophobic core in Ros. Surprisingly, the Cys2His2 zinc coordination sphere is generally poorly conserved in the Ros homologues, raising the question of whether the zinc ion is always preserved in these proteins. Here, we present a functional and structural study of a point mutant of Ros protein, Ros56–142C82D, in which the second coordinating cysteine is replaced by an aspartate, 5 previously-uncharacterized representative Ros homologues from Mesorhizobium loti, and 2 mutants of the homologues. Our results indicate that the prokaryotic zinc-finger domain, which in Ros protein tetrahedrally coordinates Zn(II) through the typical Cys2His2 coordination, in Ros homologues can either exploit a CysAspHis2 coordination sphere, previously never described in DNA binding zinc finger domains to our knowledge, or lose the metal, while still preserving the DNA-binding activity. We demonstrate that this class of prokaryotic zinc-finger domains is structurally very adaptable, and surprisingly single mutations can transform a zinc-binding domain into a nonzinc-binding domain and vice versa, without affecting the DNA-binding ability. In light of our findings an evolutionary link between the prokaryotic and eukaryotic zinc-finger domains, based on bacteria-to-eukaryota horizontal gene transfer, is discussed.

A gene that encodes a protein consisting solely of zinc finger domains is preferentially expressed in transformed mouse cells

1990 ◽  
Vol 10 (1) ◽  
pp. 418-421
Author(s):  
M Ernoult-Lange ◽  
M Kress ◽  
D Hamer
Keyword(s):  
Amino Acids ◽  
Brain Tissue ◽  
Zinc Finger ◽  
Cellular Transformation ◽  
Zinc Finger Proteins ◽  
Mouse Cells ◽  
Zinc Finger Domains ◽  
Transformed Cell Lines ◽  
Testis Tissue

We describe the cloning and characterization of the mouse MOK-2 gene, a new member of the Krüppel family of zinc finger proteins. Sequencing of both cDNA and genomic clones showed that the predicted MOK-2 protein consists of seven zinc finger domains with only five additional amino acids. The finger domains of MOK-2 are highly homologous to one another but not to those of other zinc finger proteins. MOK-2 is preferentially expressed in transformed cell lines, brain tissue, and testis tissue. Its possible role in cellular transformation is discussed.

scholarly journals Purification of proteins containing zinc finger domains using immobilized metal ion affinity chromatography

2011 ◽  
Vol 79 (1) ◽  
pp. 88-95 ◽  
Author(s):  
Irena Voráčková ◽  
Šárka Suchanová ◽  
Pavel Ulbrich ◽  
William E. Diehl ◽  
Tomáš Ruml
Keyword(s):  
Affinity Chromatography ◽  
Zinc Finger ◽  
Metal Ion ◽  
Zinc Finger Domains ◽  
Metal Ion Affinity Chromatography

scholarly journals Synthesis and characterization of some biological active transition metal complexes of Schiff base derived from cefixime with mixed ligand 8-hydroxy quinoline

2015 ◽  
Vol 12 (4) ◽  
pp. 797-807
Author(s):  
Baghdad Science Journal
Keyword(s):  
Melting Point ◽  
Metal Ion ◽  
Bidentate Ligand ◽  
Mixed Ligand ◽  
Molar Ratio ◽  
Synthesis And Characterization ◽  
Vis Spectroscopy ◽  
Ft Ir ◽  
Hydroxy Quinoline

The aim of the work is synthesis and characterization of bidentate ligand [dipotassium sodium7-((E)-2-(2-((Z)-1-carboxylatoethylideneamino)thiazol-4-yl)-2 (carboxylatemethoxyimino) acet amido)-8-oxo-3-vinyl-5- thia-1-azabicyclo[4.2.0] oct-2- ene-2- carboxylate] [Nak2L], from the reaction of cefixime with sodium pyruvet to produce the ligand [Nak2L], the reaction was carried out in methanol as a solvent under reflux. The prepared ligand [Nak2L] which was characterized by FT-IR, UV-Vis spectroscopy, 1H, 13C-NMR spectra, Mass spectra, (C.H.N) and melting point. The mixed ligand complexes were prepared from ligand [Nak2L] was used as a primary ligand while 8-hydroxy quinoline [Q] was used as a secondary ligand with metal ion M(?).Where M(?) = (Mn ,Co ,Ni ,Cu ,Zn and Cd) at reflux ,using methanol as a solvent, KOH as a base. Complexes of the composition [(M)2(Q)2(KL)(H2O)4] with (2:2:1) molar ratio were prepared. All the complexes were characterized by spectroscopic methods (FT-IR, UV-Vis spectroscopy) along with elemental analysis (A.A), chloride content and melting point measurements were carried out, together with conductivity and magnetic susceptibility. These measurements showed octahedral geometry around (Mn??, Co??, Ni??, Cu??, Zn?? and Cd??) ions. The biological activity of the ligands [NaK2L], [Q] and complexes [(M)2(Q)2(KL)(H2O)4] were studied by using inhibition method.

scholarly journals A gene that encodes a protein consisting solely of zinc finger domains is preferentially expressed in transformed mouse cells.

1990 ◽  
Vol 10 (1) ◽  
pp. 418-421 ◽  
Author(s):  
M Ernoult-Lange ◽  
M Kress ◽  
D Hamer
Keyword(s):  
Amino Acids ◽  
Brain Tissue ◽  
Zinc Finger ◽  
Cellular Transformation ◽  
Zinc Finger Proteins ◽  
Mouse Cells ◽  
Zinc Finger Domains ◽  
Transformed Cell Lines ◽  
Testis Tissue

We describe the cloning and characterization of the mouse MOK-2 gene, a new member of the Krüppel family of zinc finger proteins. Sequencing of both cDNA and genomic clones showed that the predicted MOK-2 protein consists of seven zinc finger domains with only five additional amino acids. The finger domains of MOK-2 are highly homologous to one another but not to those of other zinc finger proteins. MOK-2 is preferentially expressed in transformed cell lines, brain tissue, and testis tissue. Its possible role in cellular transformation is discussed.

Synthesis and Characterization of A New Weak Ferromagnet: Fe(II) Ethylene-BIS-(Phosphonates)

1998 ◽  
Vol 547 ◽  
Author(s):  
C. Bellitto ◽  
F. Federici ◽  
M.R. Mahmoud ◽  
S.A. Ibrahim
Keyword(s):  
Metal Ion ◽  
Three Dimensional ◽  
Electronic Configuration ◽  
Antiferromagnetic Order ◽  
Zero Field ◽  
Thermal Variation ◽  
Weak Ferromagnet ◽  
Uv Visible ◽  
Spin Electronic

AbstractIron(II)-ethylene-bis-(phosphonates), Fe2[O3P-(CH2)2-PO3]·2H2O was synthesized by reaction of [FeSO4]·7H2O and the corresponding ethylene-bis-(phosphonic acid) and it was characterized by X-ray powder diffraction, thermogravimetry, UV-visible and infrared spectroscopy, and the magnetic properties were studied by a SQUID magnetometer. The metal-ion is in the d6 high-spin electronic configuration and it appears to have an octahedral coordination. The thermal variation of the d.c. magnetic susceptibility of Fe2[O3P-(CH2)2-PO3]·2H2O follows the Curie-Weiss law, with a negative Weiss constant of θ =-55K. Below 100K, the susceptibility increases until a peak at TN=24K is observed, and this is associated to the three-dimensional antiferromagnetic order. Below 24K, Fe2[O3P-(CH2)2-PO3]·2H2O behaves as a “weak” ferromagnet and it represents an example of an unusual kind of molecular-based magnetic materials, having a finite zero-field magnetization.

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