Kapoor, Shobhna and Mandal, Soumit S and Bhattacharyya, Aninda Jiban (2009) Structure and Function of Hemoglobin Confined Inside Silica Nanotubes. In: Journal of physical chemistry B, 113 (43). pp. 14189-14195.
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Investigations on the structure and function of hemoglobin (Hb) confined inside sol-gel template synthesized silica nanotubes (SNTs) have been discussed here. Immobilization of hemoglobin inside SNTs resulted in the enhancement of direct electron transfer during an electrochemical reaction. Extent of influence of nanoconfinement on protein activity is further probed via ligand binding and thermal stability studies. Electrochemical investigations show reversible binding of n-donor liquid ligands, such as pyridine and its derivatives, and predictive variation in their redox potentials suggests an absence of any adverse effect on the structure and function of Hb confined inside nanometer-sized channels of SNTs. Immobilization also resulted in enhanced thermal stability of Hb. The melting or denaturation temperature of Hb immobilized inside SNTs increase by approximately 4 degrees C as compared with that of free Hb in solution.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to American Chemical Society.|
|Department/Centre:||Division of Chemical Sciences > Solid State & Structural Chemistry Unit|
|Date Deposited:||03 Jan 2010 09:18|
|Last Modified:||19 Sep 2010 05:52|
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