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IJC-A Vol.50A(03-04) [March-April 2011] >


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)(H2O)2]ClO4 (1), Na[Cr(EDTA)(H2O)] (2) and [Cr(en)3]Cl3 (3) 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 (1) and (2) 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 (3) 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 (1), (2) and (3). CD spectrum of BSA clearly indicates that binding of (1) and (2) leads to increase in the helicity of BSA, whereas binding of (3) 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 411 and Arg 410) 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.
Page(s): 531-538
CC License:  CC Attribution-Noncommercial-No Derivative Works 2.5 India
ISSN: 0975-0975(Online); 0376-4710(Print)
Source:IJC-A Vol.50A(03-04) [March-April 2011]

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