Designed protein aggregates entrapping carbon nanotubes for bioelectrochemical oxygen reduction
Abstract
The engineering of robust protein/nanomaterial interfaces is critical in the development of bioelectrocatalytic systems. We have used computational protein design to identify two amino acid mutations in the small laccase protein (SLAC) from Streptomyces coelicolor to introduce new inter‐protein disulfide bonds. The new dimeric interface introduced by these disulfide bonds in combination with the natural trimeric structure drive the self‐assembly of SLAC into functional aggregates. The mutations had a minimal effect on kinetic parameters, and the enzymatic assemblies exhibited an increased resistance to irreversible thermal denaturation. The SLAC assemblies were combined with single‐walled carbon nanotubes (SWNTs), and explored for use in oxygen reduction electrodes. The incorporation of SWNTs into the SLAC aggregates enabled operation at an elevated temperature and reduced the reaction overpotential. A current density of 1.1 mA/cm2 at 0 V versus Ag/AgCl was achieved in an air‐breathing cathode system. Biotechnol. Bioeng. 2016;113: 2321–2327. © 2016 Wiley Periodicals, Inc.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Sep 20, 2016
- Source ID
- 10.1002/bit.25996
Entities
People
- David Baker
- Kristen E. Garcia
- Mansij Hans
- Plamen Atanassov
- Scott Banta
- Sofia Babanova
- William Scheffler
Organizations
- Air Force Office of Scientific Research
- Columbia University
- University of New Mexico
- University of Washington