Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/11251
Title: Chromium(III) mediated conformational changes associated with alterations in the enzymatic activity of BSA: Influence of the coordinated ligand
Authors: Raja, Natesasn Sella
Shrivastava, H Yamini
Nair, Balachandran Unni
Keywords: Bioinorganic chemistry
Metalloproteins
Chromium
Tryptic digestion
Circular dichroism
Bovine serum albumin
Issue Date: Mar-2011
Publisher: NISCAIR-CSIR, India
Abstract: Interaction of three chromium(III) complexes, [Cr(salen)(H<sub>2</sub>O)<sub>2</sub>]ClO<sub>4 </sub><b>(1)</b>, Na[Cr(EDTA)(H<sub>2</sub>O)] <b>(2)</b> and [Cr(en)<sub>3</sub>]Cl<sub>3</sub> <b>(3)</b> with bovine serum albumin (BSA) has been investigated in order to understand the role of coordinated ligand in mediating the interaction between the protein and chromium(III) ion. Binding of <b>(1)</b> and <b>(2)</b> to BSA has been found to result in increase in the esterase activity of BSA from 2.41 to 2.72 and 2.62 U/L respectively. On the other hand, binding of <b>(3)</b> results in decrease of the activity from 2.41 to 1.91 U/L. These changes in the esterase activity are also reflected in the conformation of BSA in the presence of <b>(1)</b>, <b>(2)</b> and <b>(3)</b>. CD spectrum of BSA clearly indicates that binding of <b>(1)</b> and <b>(2)</b> leads to increase in the helicity of BSA, whereas binding of <b>(3)</b> leads to decrease in the helicity of the protein. Such a change in the helicity of BSA leads to change in the orientation of active amino acids (Tyr <sub>411</sub> and Arg <sub>410</sub>) in the protein, thus affecting the esterase activity of protein. The nature of the coordinated ligand has also been found to influence the stability of BSA against trypsin digestion.
Description: 531-538
URI: http://hdl.handle.net/123456789/11251
ISSN: 0975-0975(Online); 0376-4710(Print)
Appears in Collections:IJC-A Vol.50A(03-04) [March-April 2011]

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