Transition metal ion binding studies of carnosine and histidine: Biologically relevant antioxidants

2008 ◽  
Vol 66 (2) ◽  
pp. 291-294 ◽  
Author(s):  
Stephanie Velez ◽  
Nanditha G. Nair ◽  
V. Prakash Reddy
Keyword(s):  
Transition Metal ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies ◽  
Transition Metal Ion ◽  
Biologically Relevant

scholarly journals The src Homology 3-Like Domain of the Diphtheria Toxin Repressor (DtxR) Modulates Repressor Activation through Interaction with the Ancillary Metal Ion-Binding Site

2003 ◽  
Vol 185 (7) ◽  
pp. 2251-2258 ◽  
Author(s):  
John F. Love ◽  
Johanna C. vanderSpek ◽  
John R. Murphy
Keyword(s):  
Transition Metal ◽  
Binding Site ◽  
Diphtheria Toxin ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies ◽  
Transition Metal Ion ◽  
Diphtheria Toxin Repressor

ABSTRACT The diphtheria toxin repressor (DtxR) is a transition metal ion-activated repressor that acts as a global regulatory element in the control of iron-sensitive genes in Corynebacterium diphtheriae. We recently described (L. Sun, J. C. vanderSpek, and J. R. Murphy, Proc. Natl. Acad. Sci. USA 95:14985-14990, 1998) the isolation and in vivo characterization of a hyperactive mutant of DtxR, DtxR(E175K), that appeared to be constitutively active. We demonstrate here that while DtxR(E175K) remains active in vivo in the presence of 300 μM 2,2′dipyridyl, the purified repressor is, in fact, dependent upon low levels of transition metal ion to transit from the inactive apo form to the active metal ion-bound form of the repressor. Binding studies using 8-anilino-1-naphthalenesulfonic acid suggest that the E175K mutation stabilizes an intermediate of the molten-globule form of the repressor, increasing exposure of hydrophobic residues to solvent. We demonstrate that the hyperactive DtxR(E175K) phenotype is dependent upon an intact ancillary metal ion-binding site (site 1) of the repressor. These observations support the hypothesis that metal ion binding in the ancillary site facilitates the conversion of the inactive apo-repressor to its active, operator-binding conformation. Furthermore, these results support the hypothesis that the C-terminal src homology 3-like domain of DtxR plays an active role in the modulation of repressor activity.

Thermodynamics of Transition Metal Ion Binding to Proteins

2020 ◽  
Vol 142 (13) ◽  
pp. 6365-6374 ◽  
Author(s):  
Lin Frank Song ◽  
Arkajyoti Sengupta ◽  
Kenneth M. Merz
Keyword(s):  
Transition Metal ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Transition Metal Ion

An investigation into transition metal ion binding properties of silk fibers and particles using radioisotopes

2010 ◽  
Vol 119 (6) ◽  
pp. 3630-3639 ◽  
Author(s):  
Rangam Rajkhowa ◽  
Radhika Naik ◽  
Lijing Wang ◽  
Suzanne V. Smith ◽  
Xungai Wang
Keyword(s):  
Transition Metal ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Properties ◽  
Transition Metal Ion ◽  
Silk Fibers

Bromine substituted aminonaphthoquinones: synthesis, characterization, DFT and metal ion binding studies

RSC Advances ◽  
2016 ◽  
Vol 6 (91) ◽  
pp. 88010-88029 ◽  
Author(s):  
Gunjan Agarwal ◽  
Dipali N. Lande ◽  
Debamitra Chakrovarty ◽  
Shridhar P. Gejji ◽  
Prajakta Gosavi-Mirkute ◽  
...  
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies

Bromine substituted aminonaphthoquinones – chemosensors for metal ions.

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