Metal ion interactions with bovine prothrombin and prothrombin fragment. 1. Stoichiometry of binding, protein self-association, and conformational change induced by a variety of metal ions

Biochemistry ◽  
1981 ◽  
Vol 20 (2) ◽  
pp. 351-358 ◽  
Author(s):  
Gary L. Nelsestuen ◽  
Robert M. Resnick ◽  
G. Jason Wei ◽  
Carol H. Pletcher ◽  
Victor A. Bloomfield
Keyword(s):  
Metal Ions ◽  
Conformational Change ◽  
Metal Ion ◽  
Binding Protein ◽  
Prothrombin Fragment ◽  
Ion Interactions ◽  
Self Association ◽  
Metal Ion Interactions

DNA-bound metal ions: recent developments

2014 ◽  
Vol 5 (5) ◽  
pp. 397-407 ◽  
Author(s):  
Daniel L. Morris
Keyword(s):  
Dna Damage ◽  
Metal Ions ◽  
Recent Work ◽  
Conformational Changes ◽  
Metal Ion ◽  
Oxidative Dna Damage ◽  
Logic Gates ◽  
Base Pairing ◽  
Ion Interactions ◽  
Metal Ion Interactions

AbstractThe affinity of metal ions for DNA is logical considering that the structure of DNA includes a phosphate backbone with a net-negative charge, a deoxyribose sugar with O atoms, and purine and pyrimidine bases that contain O and N atoms. DNA-metal ion interactions encompass a large area of research that ranges from the most fundamental characterization of DNA-metal ion binding to the role of DNA-bound metal ions in disease and human health. Alternative DNA base pairing mediated by metal binding is also being investigated and manipulated for applications in logic gates, molecular machines, and nanotechnology. This review highlights recent work aimed at understanding interactions of redox-active metal ions with DNA that provides a better understanding of the mechanisms by which various types of oxidative DNA damage (strand breakage and base modifications) occur. Antioxidants that mitigate oxidative DNA damage by coordinating metal ions that produce reactive oxygen species are addressed, as well as recent work on the effect of DNA-metal ion interactions and the efficacy of quinolone-based antibacterial drugs. Recent advances in metal-mediated base pairing that triggers conformational changes in DNA structure for use as selective metal ion sensors and novel nanotechnology applications are also included.

scholarly journals Metal ion interactions in the control of haem oxygenase induction in liver and kidney

1980 ◽  
Vol 192 (2) ◽  
pp. 637-648 ◽  
Author(s):  
G S Drummond ◽  
A Kappas
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Simultaneous Administration ◽  
Ion Interactions ◽  
Liver And Kidney ◽  
Demethylase Activity ◽  
Haem Oxygenase ◽  
Metal Ion Interactions ◽  
Cytochrome P 450

Mn2+ and Zn2+ exhibit a striking ability to block the induction by Sn2+ and Ni2+ of haem oxygenase (EC 1.14.99.3) in kidney. The blocking effects of Mn2+ and Zn2+ were found to be greatest on simultaneous administration, time-dependent when administered up to 8 h before the inducing metal ions, and ineffective when administered as little as 10 min after the inducing metal ions. The decreases in cytochrome P-450 and haem contents and the sequential changes in delta-aminolaevulinate synthase (EC 2.3.1.37) activity that occur concomitant with haem oxygenase induction were largely eliminated with simultaneous or prior treatment with Mn2+ or Zn2+, but not when Mn2+ or Zn2+ was administered after Sn2+ or Ni2+. Mn2+ and Zn2+ did not increase the catabolism of the enzyme in vivo. Zn2+ on simultaneous administration was also able substantially to block the induction of haem oxygenase by Co2+, Cd2+ and Ni2+ in liver. The Zn2+ blockade of Cd2+ induction was examined in detail, and prior or simultaneous administration of Zn2+ was found to be effective in blocking the induction of haem oxygenase and the concomitant decreases in cytochrome P-450 and haem contents, ethylmorphine demethylase activity and the sequential changes in delta-aminolaevulinate synthase activity. Zn2+ administration 10 min or more after Cd2+ was ineffective in preventing the occurrence of these perturbations in haem metabolism. These findings describe a new and striking biological property of Mn2+ and Zn2+, and indicate the existence of significant metal ion interactions in the control of haem metabolism.

Sign in / Sign up

Export Citation Format

Share Document