Immobilized enzymes as catalytically-active tools for nanofabrication

Journal of the American Chemical Society

Volumn 124, Issue 41, 2002, Pages 12114-12115

  Jang, Chang Hyun ^a   Stevens, Benjamin D ^a,b   Carlier, Paul R ^a   Calter, Michael A ^a,b   Ducker, William A ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^b UNIVERSITY OF ROCHESTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CATALYSIS; CATALYST; ENZYME IMMOBILIZATION; MATERIALS; NANOTECHNOLOGY; SYNTHESIS;

EID: 0037120841     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja017686v     Document Type: Article

References (17)

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12. We confirmed the activity of the enzyme after immobilization by immobilizing the enzyme on the entire surface of a gold ball, and exposing a solution of 7-acetoxy-1-methylquinolinium iodide (AMQI) to the gold ball. The hydrolysis product of AMQI was visible by fluorescence microscopy.
13. -1, and the molar mass is about 70 kDa per catalytic site (Rosenberry, T. L. Adv. Enzymol. Relat. Areas Mol. Biol. 1975, 43, 103-218), so that the proteinaceous material contains 7-15% active AChE. The exterior of Electrophorus electricus AChE presents eight lysines that have amino groups available for tethering (Bourne Y.; Grassi J.; Bourgis, P. E.; Marchot, P. J. Biol. Chem. 1999, 274. 30370-30376. PDB codes 1C2B and 1C20). The effect of tethering on catalytic activity is unknown.
14. -1, and the molar mass is about 70 kDa per catalytic site (Rosenberry, T. L. Adv. Enzymol. Relat. Areas Mol. Biol. 1975, 43, 103-218), so that the proteinaceous material contains 7-15% active AChE. The exterior of Electrophorus electricus AChE presents eight lysines that have amino groups available for tethering (Bourne Y.; Grassi J.; Bourgis, P. E.; Marchot, P. J. Biol. Chem. 1999, 274. 30370-30376. PDB codes 1C2B and 1C20). The effect of tethering on catalytic activity is unknown.
15. Green, T. W.; Wuts, G. M. Protective Groups in Organic Synthesis, 3rd ed.; Wiley: New York, 1999; pp 482-484. Our solution was initially at pH 10 and was kept at or above pH 9 during the hydrolysis through the addition of NaOH.
16. The thiocholine molecules produce high contrast in AFM images in ethanol. When imaged using tapping mode in ethanol solution, the thiocholine molecules are about 3.9 nm "higher" than the surrounding EOthiol, even though the extended van der Waals length of the EOthiol is about 1.7 nm longer. Contrast in tapping mode arises from differences in height, force, and elasticity. In this case the contrast is probably high because we contrast the weak tail of a long-range electrostatic force of the quaternary ammonium to a shorter-range solvation force of the ethylene oxide groups. We observe similar high contrast for carboxylate groups imaged under the same conditions.
17. 2 thin film of gold to thiocholine and monitoring the adsorption by SPR (Leica).