| Title |
Self-assembling biomolecular catalysts for hydrogen production
|
|---|---|
| Published in |
Nature Chemistry, December 2015
|
| DOI | 10.1038/nchem.2416 |
| Pubmed ID | |
| Authors | |
| Abstract |
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. |
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Geographical breakdown
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| France | 1 | 3% |
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| Greece | 1 | 3% |
| Kuwait | 1 | 3% |
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| Other | 0 | 0% |
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Demographic breakdown
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|---|---|---|
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| Scientists | 6 | 19% |
| Practitioners (doctors, other healthcare professionals) | 1 | 3% |
Mendeley readers
Geographical breakdown
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|---|---|---|
| United States | 4 | 2% |
| Uruguay | 1 | <1% |
| Netherlands | 1 | <1% |
| Iran, Islamic Republic of | 1 | <1% |
| United Kingdom | 1 | <1% |
| Denmark | 1 | <1% |
| Unknown | 224 | 96% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
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| Researcher | 42 | 18% |
| Student > Bachelor | 29 | 12% |
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| Professor > Associate Professor | 12 | 5% |
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| Other | 26 | 11% |
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