By Topic

Directed Metallization of Single-Enzyme Molecules With Preserved Enzymatic Activity

Sign In

Cookies must be enabled to login.After enabling cookies , please use refresh or reload or ctrl+f5 on the browser for the login options.

Formats Non-Member Member
$31 $13
Learn how you can qualify for the best price for this item!
Become an IEEE Member or Subscribe to
IEEE Xplore for exclusive pricing!
close button

puzzle piece

IEEE membership options for an individual and IEEE Xplore subscriptions for an organization offer the most affordable access to essential journal articles, conference papers, standards, eBooks, and eLearning courses.

Learn more about:

IEEE membership

IEEE Xplore subscriptions

6 Author(s)
Vernick, S. ; Dept. of Phys. Electron., Tel Aviv Univ., Tel Aviv ; Moscovich-Dagan, H. ; Porat-Ophir, C. ; Rishpon, Judith
more authors

A new method for the fabrication of molecular, water-soluble, and biologically active enzyme-metal hybrids was designed and its feasibility demonstrated. The method is based on the display of nucleation sites directing a subsequent electroless deposition of palladium and other metals to the enzyme's surface. The process is carried out under mild physiological conditions, enabling the preservation of enzymatic activity and water solubility. The feasibility of the new method was demonstrated by using the enzyme glucose oxidase and palladium combination as the first model system. The glucose oxidase-palladium hybrid thus obtained retained their solubility and enzymatic glucose oxidation capabilities. Hybrids immobilized on platinum electrodes exhibited ldquonanowiringrdquo and effective direct electron transfer from the enzyme catalytic site to the electrode. The new enzyme-metal hybrids thus obtained may be readily incorporated into miniaturic biosensors and biochips, used as novel antibacterial agents or as markers for improved in vivo imaging. Furthermore, the methodology developed may be readily extended to a series of metal coatings on the surface of biologically active proteins.

Published in:

Nanotechnology, IEEE Transactions on  (Volume:8 ,  Issue: 1 )