Structure and function of hemoglobin confined inside silica nanotubes

Kapoor, Shobhna ; Mandal, Soumit S. ; Bhattacharyya, Aninda J. (2009) Structure and function of hemoglobin confined inside silica nanotubes The Journal of Physical Chemistry B, 113 (43). pp. 14189-14195. ISSN 1520-6106

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Official URL: http://pubs.acs.org/doi/abs/10.1021/jp9032707

Related URL: http://dx.doi.org/10.1021/jp9032707

Abstract

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 °C as compared with that of free Hb in solution.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:108304
Deposited On:22 Dec 2017 10:09
Last Modified:22 Dec 2017 10:09

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