Mixed-valence chemistry of adjacent vanadium centers in heteropolytungstate anions. I. Synthesis and electronic structures of mono-, di-, and trisubstituted derivatives of .alpha.-octadecatungstodiphosphate(6-) ion (.alpha.-[P2W18O62]6-)

1983 ◽  
Vol 105 (13) ◽  
pp. 4286-4292 ◽  
Author(s):  
Subhash P. Harmalker ◽  
Michele A. Leparulo ◽  
Michael T. Pope
Keyword(s):  
Electronic Structures ◽  
Mixed Valence ◽  
Derivatives Of

ChemInform Abstract: Molecular and Electronic Structures of Mixed-Valence exo,exo-1,12-Dimethyl[1.1]ferrocenophanium Triiodide

1986 ◽  
Vol 17 (17) ◽  
Author(s):  
M. F. MOORE ◽  
S. R. WILSON ◽  
M. J. COHN ◽  
T.-Y. DONG ◽  
U. T. MUELLER-WESTERHOFF ◽  
...  
Keyword(s):  
Electronic Structures ◽  
Mixed Valence

Molecular and electronic structures of mixed-valence exo,exo-1,12-dimethyl[1.1]ferrocenophanium triiodide

1985 ◽  
Vol 24 (26) ◽  
pp. 4559-4565 ◽  
Author(s):  
Michael F. Moore ◽  
Scott R. Wilson ◽  
Michelle J. Cohn ◽  
Teng Yuan Dong ◽  
Ulrich T. Mueller-Westerhoff ◽  
...  
Keyword(s):  
Electronic Structures ◽  
Mixed Valence

Electrostatic and Conformational Effects on the Electronic Structures of Distortional Isomers of a Mixed-Valence Binuclear Cu Complex

2001 ◽  
Vol 40 (25) ◽  
pp. 6375-6382 ◽  
Author(s):  
Stefan Franzen ◽  
Vincent M. Miskowski ◽  
Andrew P. Shreve ◽  
Stacie E. Wallace-Williams ◽  
William H. Woodruff ◽  
...  
Keyword(s):  
Electronic Structures ◽  
Mixed Valence ◽  
Cu Complex ◽  
Conformational Effects

scholarly journals The influence of metals of variable valence on the oxidative modification of albumin amino acid residues

2021 ◽  
Vol 9 (3) ◽  
pp. 369-376
Author(s):  
O.A. Zav’yalova ◽  
◽  
Yu.A. Marsyanova ◽  
Yu.V. Abalenikhinа ◽  
A.F. Ishtulin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Mixed Valence ◽  
Oxidative Modification ◽  
Amino Acid Residues ◽  
Variable Valence ◽  
Carbonyl Derivatives ◽  
Derivatives Of

BACKGROUND: The constancy of the protein composition of the body is one of the most important conditions for normal vital activity. Deviations in the content of the main bioelements, in particular, mixed valence metals, caused by environmental factors, improper nutrition and other factors, lead to various disorders. One of the properties of metals of mixed valence is the abil-ity to cause metal-catalyzed oxidation of proteins in joint action with active forms of oxygen. It seems interesting to study the oxidative modification of the amino acid residues of albumin and the change in its properties. AIM: To study the effect of reactive oxygen intermediates generated by the Fenton reaction in the presence of Fe2+ and Cu2+ on the oxidative modification of amino acid residues of bovine serum albumin. MATERIALS AND METHODS: The study was carried out on bovine serum albumin (BSA), which was incubated for 2 hours in a mixture of Fenton's reagents – FeSO4 + H2O2 and in a mixture of СuSO4 + H2O2. The quantitative protein content in the samples was determined with the bromcresol green reagent (Albumin-Olvex). The content of carbonyl derivatives of proteins was estimated by the method of R.L. Levine modified by E.E. Dubinina. The content of thiol groups in albumin samples from the control and experimental groups was determined by the Ellman method with DTNB (under non-denaturing conditions. RESULTS: The presented results demonstrate that under the action of Cu2+ ions, the formation of carbonyl derivatives of aliphatic amino acids of albumin is less than in the presence of Fe2+, which can be explained by the different degrees of albumin affinity to metals of variable valence. The rate of mobility of oxidatively modified albumin in polyacrylamide gel decreases, which is explained by protein aggregation due to bityrosine cross-links. CONCLUSION: Variable valence metals affect the modification of albumin. The change in the functional properties of the protein is of physiological significance, including the case of extracellular mobilization of iron and copper.

Sign in / Sign up

Export Citation Format

Share Document