Stability constants and spectral studies of complexes of 2-hydroxy-5-methylazobenzene-2′-carboxylic acid with some divalent metal ions

1984 ◽  
Vol 62 (11) ◽  
pp. 2299-2301
Author(s):  
C. Mahalingam ◽  
J. K. Sthapak ◽  
D. D. Sharma ◽  
R. L. Tiwari ◽  
Smita Sthapak

The stability constants of metal complexes of 2-hydroxy-5-methylazobenzene-2′-carboxylic acid have been determined spectrophotometrically. These follow the Irving–Williams sequence: log KOH(H) = 10.67, log K1(Co) = 9.02, log K1(Ni) = 9.68, log K1(Cu) = 13.37, log K1(Zn) = 7.58, and [Formula: see text]The chelates of Mn(II), Fe(II), Co(II), Ni(II), Cu(II), Zn(II), and [Formula: see text] with the dye have been prepared and characterized on the basis of their ir and reflectance spectra.

1962 ◽  
Vol 15 (4) ◽  
pp. 786 ◽  
Author(s):  
RW Green ◽  
GKS Ooi

Spectrophotometric and pH-titration methods have been used to determine the stability constants at 25 �C of complexes between transition metal ions and the anion of 6-hydroxymethylpyridine-2-carboxylic acid. This anion is found to be a weaker base and a weaker complexing agent than the pyridine-2-carboxylate ion. There is some evidence for steric hindrance of tris complexes.


2011 ◽  
Vol 55 (6) ◽  
pp. 2905-2915 ◽  
Author(s):  
Eric B. Lansdon ◽  
Qi Liu ◽  
Stephanie A. Leavitt ◽  
Mini Balakrishnan ◽  
Jason K. Perry ◽  
...  

ABSTRACTHIV-1 RNase H breaks down the intermediate RNA-DNA hybrids during reverse transcription, requiring two divalent metal ions for activity. Pyrimidinol carboxylic acid andN-hydroxy quinazolinedione inhibitors were designed to coordinate the two metal ions in the active site of RNase H. High-resolution (1.4 Å to 2.1 Å) crystal structures were determined with the isolated RNase H domain and reverse transcriptase (RT), which permit accurate assessment of the metal and water environment at the active site. The geometry of the metal coordination suggests that the inhibitors mimic a substrate state prior to phosphodiester catalysis. Surface plasmon resonance studies confirm metal-dependent binding to RNase H and demonstrate that the inhibitors do not bind at the polymerase active site of RT. Additional evaluation of the RNase H site reveals an open protein surface with few additional interactions to optimize active-site inhibitors.


2012 ◽  
Vol 28 (07) ◽  
pp. 1714-1720 ◽  
Author(s):  
NI Zhe-Ming ◽  
◽  
LIU Jiao ◽  
XUE Ji-Long ◽  
LI Yuan ◽  
...  

1969 ◽  
Vol 47 (12) ◽  
pp. 2320-2323 ◽  
Author(s):  
Vedula S. Sastri ◽  
Keijo I. Aspila ◽  
Chuni L. Chakrabarti

Studies on the solvent extraction of morpholine dithiocarbamic acid complexes of divalent metal ions Mn, Fe, Co, Ni, Cu, Zn, Pb, Cd, Hg, and Sn were carried out, and the extraction constants and the overall stability constants were determined. The stability constants of complexes of Cu(II) formed with various substituted dithiocarbamic acids, showed a variation of the stability constants with the basicity of the nitrogen and sulfur atoms in the reagents.


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