Self-assembling biomolecular catalysts for hydrogen production

The chemistry of highly evolved protein-based compartments has inspired the design of new catalytically active materials that self-assemble from biological components. A frontier of this biodesign is the potential to contribute new catalytic systems for the production of sustainable fuels, such as h...

Full description

Saved in:
Bibliographic Details
Published in:Nature chemistry 2016-02, Vol.8 (2), p.179-185
Main Authors: Jordan, Paul C., Patterson, Dustin P., Saboda, Kendall N., Edwards, Ethan J., Miettinen, Heini M., Basu, Gautam, Thielges, Megan C., Douglas, Trevor
Format: Article
Language:English
Subjects:
631/61/350
639/638/298/54/989
639/638/541/966
639/638/77/603
Analytical Chemistry
Biochemistry
Catalysis
Chemistry
Chemistry/Food Science
E coli
Escherichia coli
Escherichia coli - chemistry
Hydrogen - chemistry
Hydrogen production
Hydrogenase - chemistry
Inorganic Chemistry
Organic Chemistry
Physical Chemistry
Sustainable production
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The chemistry of highly evolved protein-based compartments has inspired the design of new catalytically active materials that self-assemble from biological components. A frontier of this biodesign is the potential to contribute new catalytic systems for the production of sustainable fuels, such as hydrogen. Here, we show the encapsulation and protection of an active hydrogen-producing and oxygen-tolerant [NiFe]-hydrogenase, sequestered within the capsid of the bacteriophage P22 through directed self-assembly. We co-opted Escherichia coli for biomolecular synthesis and assembly of this nanomaterial by expressing and maturing the EcHyd-1 hydrogenase prior to expression of the P22 coat protein, which subsequently self assembles. By probing the infrared spectroscopic signatures and catalytic activity of the engineered material, we demonstrate that the capsid provides stability and protection to the hydrogenase cargo. These results illustrate how combining biological function with directed supramolecular self-assembly can be used to create new materials for sustainable catalysis. The encapsulation and stabilization of an oxygen tolerant [NiFe]-hydrogenase, sequestered within the bacteriophage P22 capsid, has now been achieved through a directed self-assembly process. Probing the catalytic activity and infrared spectroscopic signatures of the bio-inspired assembly shows that the capsid provides stability and protection to the hydrogenase cargo.
ISSN:1755-4330
1755-4349
DOI:10.1038/nchem.2416