Structure and function of hemoglobin confined inside silica nanotubes.
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.
Kapoor
Shobhna
S
Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore 560012, India.
Mandal
Soumit S
SS
Bhattacharyya
Aninda J
AJ
D004566:Electrodes; D004579:Electron Transport; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D055767:Immobilized Proteins / Q000737:chemistry / Q000378:metabolism; D043942:Nanotubes / Q000737:chemistry*; D010084:Oxidation-Reduction; D011725:Pyridines / Q000737:chemistry; D012822:Silicon Dioxide / Q000737:chemistry*; D013696:Temperature
D006454:Hemoglobins; D055767:Immobilized Proteins; D011725:Pyridines; D012822:Silicon Dioxide; C023666:pyridine