Hydrogen fuel cells may have just taken a giant leap forward. Indiana University scientists just announced they’ve managed to create a highly efficient biomaterial that takes in protons and “spits out” hydrogen gas. Called “P22-Hyd,” this modified enzyme can be grown using a simple room temperature fermentation process — making it much more eco-friendly and considerably cheaper than the materials currently used in fuel cells, like platinum.
In a press release, lead author of the study Trevor Douglas noted, “This material is comparable to platinum, except it’s truly renewable. You don’t need to mine it; you can create it at room temperature on a massive scale using fermentation technology; it’s biodegradable. It’s a very green process to make a very high-end sustainable material.”
The way the enzyme is created is interesting in its own right. Researchers use two genes from E. coli bacteria inserted into the capsid, or viral protein shell, of a second virus. These genes then produce hydrogenase, the enzyme used to set off the hydrogen reaction.
This may sound a little complicated — and it is. Douglas admits that in the past, it’s been hard to harness hydrogenase for biofuel production due to its sensitivity to environmental conditions like warm temperatures. This new method creates enzymes that are much more stable, allowing it to be used more efficiently. Hopefully this discover will help drive down the cost of hydrogen cars — currently the vehicles retail for between $50,000 and $100,000.
Scientists at Indiana University have created a highly efficient biomaterial that catalyzes the formation of hydrogen—one half of the “holy grail” of splitting H2O to make hydrogen and oxygen for fueling cheap and efficient cars that run on water.
A modified enzyme that gains strength from being protected within the protein shell—or “capsid”—of a bacterial virus, this new material is 150 times more efficient than the unaltered form of the enzyme.
The process of creating the material was recently reported in “Self-assembling biomolecular catalysts for hydrogen production” in the journal Nature Chemistry.
“Essentially, we’ve taken a virus’s ability to self-assemble myriad genetic building blocks and incorporated a very fragile and sensitive enzyme with the remarkable property of taking in protons and spitting out hydrogen gas,” said Trevor Douglas, the Earl Blough Professor of Chemistry in the IU Bloomington College of Arts and Sciences’ Department of Chemistry, who led the study. “The end result is a virus-like particle that behaves the same as a highly sophisticated material that catalyzes the production of hydrogen.”
Other IU scientists who contributed to the research were Megan C. Thielges, an assistant professor of chemistry; Ethan J. Edwards, a Ph.D. student; and Paul C. Jordan, a postdoctoral researcher at Alios BioPharma, who was an IU Ph.D. student at the time of the study.
Illustration showing the release of NiFe-hydrogenase from inside the virus shell, or ‘capsid’, of bacteriophage P22. Credit: Indiana University
The genetic material used to create the enzyme, hydrogenase, is produced by two genes from the common bacteria Escherichia coli, inserted inside the protective capsid using methods previously developed by these IU scientists. The genes, hyaA and hyaB, are two genes in E. coli that encode key subunits of the hydrogenase enzyme. The capsid comes from the bacterial virus known as bacteriophage P22.
The resulting biomaterial, called “P22-Hyd,” is not only more efficient than the unaltered enzyme but also is produced through a simple fermentation process at room temperature.
The material is potentially far less expensive and more environmentally friendly to produce than other materials currently used to create fuel cells. The costly and rare metal platinum, for example, is commonly used to catalyze hydrogen as fuel in products such as high-end concept cars.
“This material is comparable to platinum, except it’s truly renewable,” Douglas said. “You don’t need to mine it; you can create it at room temperature on a massive scale using fermentation technology; it’s biodegradable. It’s a very green process to make a very high-end sustainable material.”
In addition, P22-Hyd both breaks the chemical bonds of water to create hydrogen and also works in reverse to recombine hydrogen and oxygen to generate power. “The reaction runs both ways—it can be used either as a hydrogen production catalyst or as a fuel cell catalyst,” Douglas said.
The form of hydrogenase is one of three occurring in nature: di-iron (FeFe)-, iron-only (Fe-only)- and nickel-iron (NiFe)-hydrogenase. The third form was selected for the new material due to its ability to easily integrate into biomaterials and tolerate exposure to oxygen.
NiFe-hydrogenase also gains significantly greater resistance upon encapsulation to breakdown from chemicals in the environment, and it retains the ability to catalyze at room temperature. Unaltered NiFe-hydrogenase, by contrast, is highly susceptible to destruction from chemicals in the environment and breaks down at temperatures above room temperature—both of which make the unprotected enzyme a poor choice for use in manufacturing and commercial products such as cars.
These sensitivities are “some of the key reasons enzymes haven’t previously lived up to their promise in technology,” Douglas said. Another is their difficulty to produce.
“No one’s ever had a way to create a large enough amount of this hydrogenase despite its incredible potential for biofuel production. But now we’ve got a method to stabilize and produce high quantities of the material—and enormous increases in efficiency,” he said.
The development is highly significant according to Seung-Wuk Lee, professor of bioengineering at the University of California-Berkeley, who was not a part of the study.
“Douglas’ group has been leading protein- or virus-based nanomaterial development for the last two decades. This is a new pioneering work to produce green and clean fuels to tackle the real-world energy problem that we face today and make an immediate impact in our life in the near future,” said Lee, whose work has been cited in a U.S. Congressional report on the use of viruses in manufacturing.
Beyond the new study, Douglas and his colleagues continue to craft P22-Hyd into an ideal ingredient for hydrogen power by investigating ways to activate a catalytic reaction with sunlight, as opposed to introducing elections using laboratory methods.
“Incorporating this material into a solar-powered system is the next step,” Douglas said.
More information: Paul C. Jordan et al. Self-assembling biomolecular catalysts for hydrogen production, Nature Chemistry (2015). DOI: 10.1038/nchem.2416
Combining bacterial genes, virus shell creates a highly efficient, renewable material used in generating power from water.
This is an artist’s rendering of P22-Hyd, a new biomaterial created by encapsulating a hydrogen-producing enzyme within a virus shell.
Credit: Indiana University
Scientists at Indiana University have created a highly efficient biomaterial that catalyzes the formation of hydrogen — one half of the “holy grail” of splitting H2O to make hydrogen and oxygen for fueling cheap and efficient cars that run on water.
A modified enzyme that gains strength from being protected within the protein shell — or “capsid” — of a bacterial virus, this new material is 150 times more efficient than the unaltered form of the enzyme.
The process of creating the material was recently reported in “Self-assembling biomolecular catalysts for hydrogen production” in the journal Nature Chemistry.
“Essentially, we’ve taken a virus’s ability to self-assemble myriad genetic building blocks and incorporated a very fragile and sensitive enzyme with the remarkable property of taking in protons and spitting out hydrogen gas,” said Trevor Douglas, the Earl Blough Professor of Chemistry in the IU Bloomington College of Arts and Sciences’ Department of Chemistry, who led the study. “The end result is a virus-like particle that behaves the same as a highly sophisticated material that catalyzes the production of hydrogen.”
Other IU scientists who contributed to the research were Megan C. Thielges, an assistant professor of chemistry; Ethan J. Edwards, a Ph.D. student; and Paul C. Jordan, a postdoctoral researcher at Alios BioPharma, who was an IU Ph.D. student at the time of the study.
The genetic material used to create the enzyme, hydrogenase, is produced by two genes from the common bacteria Escherichia coli, inserted inside the protective capsid using methods previously developed by these IU scientists. The genes, hyaA and hyaB, are two genes in E. coli that encode key subunits of the hydrogenase enzyme. The capsid comes from the bacterial virus known as bacteriophage P22.
The resulting biomaterial, called “P22-Hyd,” is not only more efficient than the unaltered enzyme but also is produced through a simple fermentation process at room temperature.
The material is potentially far less expensive and more environmentally friendly to produce than other materials currently used to create fuel cells. The costly and rare metal platinum, for example, is commonly used to catalyze hydrogen as fuel in products such as high-end concept cars.
“This material is comparable to platinum, except it’s truly renewable,” Douglas said. “You don’t need to mine it; you can create it at room temperature on a massive scale using fermentation technology; it’s biodegradable. It’s a very green process to make a very high-end sustainable material.”
In addition, P22-Hyd both breaks the chemical bonds of water to create hydrogen and also works in reverse to recombine hydrogen and oxygen to generate power. “The reaction runs both ways — it can be used either as a hydrogen production catalyst or as a fuel cell catalyst,” Douglas said.
The form of hydrogenase is one of three occurring in nature: di-iron (FeFe)-, iron-only (Fe-only)- and nitrogen-iron (NiFe)-hydrogenase. The third form was selected for the new material due to its ability to easily integrate into biomaterials and tolerate exposure to oxygen.
NiFe-hydrogenase also gains significantly greater resistance upon encapsulation to breakdown from chemicals in the environment, and it retains the ability to catalyze at room temperature. Unaltered NiFe-hydrogenase, by contrast, is highly susceptible to destruction from chemicals in the environment and breaks down at temperatures above room temperature — both of which make the unprotected enzyme a poor choice for use in manufacturing and commercial products such as cars.
These sensitivities are “some of the key reasons enzymes haven’t previously lived up to their promise in technology,” Douglas said. Another is their difficulty to produce.
“No one’s ever had a way to create a large enough amount of this hydrogenase despite its incredible potential for biofuel production. But now we’ve got a method to stabilize and produce high quantities of the material — and enormous increases in efficiency,” he said.
The development is highly significant according to Seung-Wuk Lee, professor of bioengineering at the University of California-Berkeley, who was not a part of the study.
“Douglas’ group has been leading protein- or virus-based nanomaterial development for the last two decades. This is a new pioneering work to produce green and clean fuels to tackle the real-world energy problem that we face today and make an immediate impact in our life in the near future,” said Lee, whose work has been cited in a U.S. Congressional report on the use of viruses in manufacturing.
Beyond the new study, Douglas and his colleagues continue to craft P22-Hyd into an ideal ingredient for hydrogen power by investigating ways to activate a catalytic reaction with sunlight, as opposed to introducing elections using laboratory methods.
“Incorporating this material into a solar-powered system is the next step,” Douglas said.
Story Source:
The above post is reprinted from materials provided by Indiana University. Note: Materials may be edited for content and length.
Journal Reference:
Paul C. Jordan, Dustin P. Patterson, Kendall N. Saboda, Ethan J. Edwards, Heini M. Miettinen, Gautam Basu, Megan C. Thielges, Trevor Douglas. Self-assembling biomolecular catalysts for hydrogen production. Nature Chemistry, 2015; DOI: 10.1038/nchem.2416
Chemists at Indiana University Bloomington have described the self-assembly of large, symmetrical molecules in bricks-and-mortar fashion, a development with potential value for the field of organic electronic devices such as field-effect transistors and photovoltaic cells.
Their paper, “Anion-Induced Dimerization of 5-fold Symmetric Cyanostars in 3D Crystalline Solids and 2D Self-Assembled Crystals,” has been published online by Chemical Communications, a journal of the Royal Society of Chemistry. It is the first collaboration by Amar Flood, the James F. Jackson Associate Professor of Chemistry, and Steven L. Tait, assistant professor of chemistry. Both are in the materials chemistry program in the IU Bloomington Department of Chemistry, part of the College of Arts and Sciences.
The article will appear as the cover article of an upcoming issue of the journal. The cover illustration was created by Albert William, a lecturer in the media arts and science program of the School of Informatics and Computing at Indiana University-Purdue University Indianapolis. William specializes in using advanced graphics and animation to convey complex scientific concepts.
This artwork will appear on the cover of Chemical Communications. It depicts the cyanostar molecules moving in solution, ordering on the surface, and stacking by anion binding. Imaging of the surface structure is performed by scanning.
Lead author of the paper is Brandon Hirsch, who earned the cover by winning a poster contest at the fall 2013 meeting of the International Symposium on Macrocyclic and Supramolecular Chemistry. Co-authors, along with Flood and Tait, include doctoral students Semin Lee, Bo Qiao and Kevin P. McDonald and research scientist Chun-Hsing Chen.
The researchers demonstrate the self-assembly and packing of a five-sided, symmetrical molecule, called cyanostar, that was developed by Flood’s IU research team. While researchers have created many such large, cyclic molecules, or macrocycles, cyanostar is unusual in that it can be readily synthesized in a “one pot” process. It also has an unprecedented ability to bind with large, negatively charged anions such as perchlorate.
“This great piece of work, with state-of-the-art studies of the assembly of some beautiful compounds pioneered by the group in Indiana, shows how anions can help organize molecules that could have very interesting properties,” said David Amabilino, nanomaterials group leader at the Institute of Materials Science of Barcelona. “Symmetry is all important when molecules pack together, and here the supramolecular aspects of these compounds with a very particular shape present tantalizing possibilities. This research is conceptually extremely novel and really interdisciplinary: It has really unveiled how anions could help pull molecules together to behave in completely new ways.”
The paper describes how cyanostar molecules bind with anions in 2-to-1 sandwich-like complexes, with anions sandwiched between two saucer-shaped cyanostars. The study shows the packing of the molecules in repeating patterns reminiscent of the two-dimensional packing of pentagons shown by artist Albrecht Durer in 1525. It further shows the packing to take place not only at but away from the surface of materials.
The future of organic electronics will rely upon packing molecules onto electrode surfaces, yet it has been challenging to get packing of the molecules away from the surface, Tait and Flood said. With this paper, they present a collaborative effort, combining their backgrounds in traditionally distinct fields of chemistry, as a new foray to achieve this goal using a bricks-and-mortar approach.
The paper relies on two complementary technologies that provide high-resolution images of molecules:
X-ray crystallography, which is being celebrated worldwide for its invention 100 years ago, can provide images of molecules from analysis of the three-dimensional crystalline solids.
Scanning tunneling microscopy, or STM, developed in 1981, shows two-dimensional packing of molecules immobilized on a surface.
The results are distinct, with submolecular views of the star-shaped molecules that are a few nanometers in diameter. (A human hair is about 100,000 nanometers thick).
Also Read: Rice University: Using Solar for H2O Splitting Technology for Clean Low-Cost Hydrogen Fuel
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