Related Experiment Video
Updated: Jul 15, 2026
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Direct electron transfer in nanostructured sol-gel electrodes containing bilirubin oxidase
James Lim1, Nicolas Cirigliano, John Wang
1Department of Materials Science and Engineering, University of California Los Angeles, Los Angeles, California 90095, USA.
Abstract:
Bilirubin oxidase encapsulated within a silica sol-gel/carbon nanotube composite electrode effectively catalyzed the reduction of molecular oxygen into water through direct electron transfer at the carbon nanotube electrode surface. In this nanocomposite approach, the silica matrix is designed to be sufficiently porous for substrate molecules to have access to the enzyme and yet provides a protective cage for immobilization without affecting biological activity. The incorporation of carbon nanotubes adds electrical connectivity and increases active electrode surface area. The standard surface electron transfer rate constant was calculated to be 59 s(-1) which indicates that the carbon nanotube side walls are primarily responsible for electron transfer. The use of direct electron transfer processes simplifies biofuel cell fabrication by eliminating the need for redox mediator and ion-conducting separators.

