EP1902130A2 - Composite nanomaterials for photocatalytic hydrogen production and methods of their use - Google Patents
Composite nanomaterials for photocatalytic hydrogen production and methods of their useInfo
- Publication number
- EP1902130A2 EP1902130A2 EP06849782A EP06849782A EP1902130A2 EP 1902130 A2 EP1902130 A2 EP 1902130A2 EP 06849782 A EP06849782 A EP 06849782A EP 06849782 A EP06849782 A EP 06849782A EP 1902130 A2 EP1902130 A2 EP 1902130A2
- Authority
- EP
- European Patent Office
- Prior art keywords
- composite material
- protein
- hydrogenase
- gel
- catalyst
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/14—Enzymes or microbial cells immobilised on or in an inorganic carrier
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0067—Oxidoreductases (1.) acting on hydrogen as donor (1.12)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P3/00—Preparation of elements or inorganic compounds except carbon dioxide
Definitions
- the present invention relates to composite materials containing hydrogenase enzymes and hydrogen-producing nanoparticles with photocatalysts for hydrogen production from renewable sources.
- Hydrogenases are highly evolved catalysts that produce hydrogen gas at rates that are the envy of synthetic chemists.
- Metal-containing hydrogenases (Erases) (Vignais et al. 2001; Peters et al. 1998, 1999; Adams et al. 1990) are produced by a variety of microorganisms where they function either in hydrogen oxidation or proton reduction according to the following reaction:
- Hydrogen oxidation is coupled to the generation of reducing equivalents to drive energy yielding or biosynthetic processes.
- some microorganisms are capable of coupling the oxidization and regeneration of electron carriers necessary for sugar oxidation to proton reduction and the production of hydrogen gas.
- the catalytic sites of most metal-containing hydrogenases consist of either di-Fe or heterometallic NiFe sites with diatomic ligands of carbon monoxide and cyanide to Fe. Hydrogenases are the only known enzymes that utilize these normally toxic compounds as integral parts of an active state of an enzyme.
- Hydrogenases like enzymes in general, are assembled to display precise organizational motifs that use their protein architecture to position and chemically poise an active site in which pathways for substrate access and product removal are key "design" features. Substrate, reductant, and product must have access to and from the catalytic site. Furthermore, continuous cycling of the catalyst requires ongoing addition of reactants and removal of products.
- the catalytic site of hydrogenase enzymes consists of unique biological metal clusters (Fe or NiFe) with carbon monoxide and cyanide ligands (Peters et al. 1998; Happe et al. 1997; Nicolet et al. 2000; Pierik et al. 1998; Volbeda et al. 1995).
- U.S. Patent No. 6,858,718 discloses a gene encoding for hydrogenase and a method for using the gene product for the microbial production of molecular hydrogen. More specifically, the invention discloses isolated nucleic acid sequences encoding a stable hydrogenase enzyme (HydA) that will catalyze the reduction of protons to form molecular hydrogen.
- HydA stable hydrogenase enzyme
- U.S. Pat. No. 4,532,210 discloses the biological production of hydrogen in an algal culture using an alternating light and dark cycle.
- the process comprises alternating a step for cultivating the alga in water under aerobic conditions in the presence of light to accumulate photosynthetic products (starch) in the alga, and a step for cultivating the alga in water under microaerobic conditions in the dark to decompose the accumulated material by photosynthesis to evolve hydrogen.
- This method uses a nitrogen gas purge technique to remove oxygen from the culture.
- U.S. Pat. No. 4,442,211 discloses that the efficiency of a process for producing hydrogen, by subjecting algae in an aqueous phase to light irradiation, is increased by culturing algae which has been bleached during a first period of irradiation in a culture medium in an aerobic atmosphere until it has regained color and then subjecting this algae to a second period of irradiation wherein hydrogen is produced at an enhanced rate.
- a reaction cell is used wherein light irradiates the culture in an environment ' which is substantially free of CO 2 and atmospheric O 2. This environment is maintained by passing an inert gas (e.g. helium) through the cell to remove all hydrogen and oxygen generated by the splitting of water molecules in the aqueous medium.
- an inert gas e.g. helium
- the present invention satisfies a long felt need to produce hydrogen on a commercial scale that has been achieved by combining knowledge from the disparate fields of enzymatic H 2 formation, photocatalytic nanomaterials, and electro/photo-chromic polymer gel technology.
- the present invention is directed to composite materials and methods of producing hydrogen from renewable sources, such as simple feedstocks.
- the present invention relates to a composite material for photocatalytic H 2 production comprising: 1) a polymer gel, 2) a photocatalyst, and 3) a protein based H 2 catalyst.
- the H 2 catalyst may be an enzyme such as a hydrogenase enzyme, which can be derived from a variety of organisms, such as microorganisms including but not limited to Clostridium pasteurianum, Laprobacter modestogalophilus, Thiocapsa reseopericina, or combinations thereof.
- the composite material can further comprise a redox mediator, such as poly viologen, and an oxygen scavenger, such as Cu(O).
- the photocatalyst can be formulated as a nanoparticle and can be encapsulated in a protein cage architecture.
- the H 2 catalyst may also be an artificial enzyme such as a hydrogenase mimic in the form of a protein cage comprising a shell and a core.
- the shell of the protein cage may comprise a protein wherein the protein is a 24 subunit protein such as a small heat shock protein (HSp).
- the core of the protein cage may comprise a metal wherein the metal is selected from the group consisting of platinum, nickel, iron, and cobalt.
- the present invention also relates to a method for producing H 2 using the composite materials of the present invention.
- the present invention provides methods of producing H 2 comprising reacting an electron donor with a composite material comprising 1) a polymer gel, 2) a photocatalyst, and 3) protein based H 2 catalyst.
- the electron donor can be obtained from a variety of sources, such as but not limited to acetic acid, citric acid, tartaric acid, ethanol, EDTA, hydfoxylami ⁇ e, and mixtures thereof.
- the electron donor can also be sulfite, thiosulfate, and dithionite.
- Figure l is a drawing of a composite material used in a hydrogen producing device.
- Figure 2 is a graph showing hydrogen production activity of C. pasteurianum (CpI) and L. modestogalophilus (Lm) hydro genases in solution and encapsulated in sol — gel: ⁇ , CpI in solution; •, CpI in sol — gel; ⁇ , Lm in solution; ⁇ , Lm in sol-gel.
- CpI C. pasteurianum
- Lm L. modestogalophilus
- Figure 3. is a graph showing temperature dependence of hydrogen production activity of C. pasteurianum (CpI) and L. modestogalophilus (Lm) hydrogenases in solution and encapsulated in sol-gel: ⁇ , CpI in solution; •, CpI in sol — gel; A, Lm in solution; ⁇ , Lm in sol-gel.
- Figure 4. is a graph showing hydrogen production activity of solution and sol-gel encapsulated hydrogenase from C. pasteurianum in the presence (open) and absence (shaded) of protease.
- Figure 5 is (A) a space filling representation of the small heat shock protein (Hsp) cage from Methano co ecus j annas chii (pdb: l shs) and (B) a cut-away view of Hsp showing the interior cavity of the cage.
- Hsp small heat shock protein
- Figure 6 is a size exclusion chromatography of Hsp: (A) unmineralized Hsp; (B) Hsp mineralized with 250 Pt/Hsp showing coelution of protein (280 nm) and mineral (350 nm); (C) Hsp mineralized with 1000 Pt/Hsp showing coelution of protein (280 nm) and mineral (350 nm).
- Figure 7 is an image showing (A) TEM of Hsp 1000 Pt unstained. The inset shows electron diffraction of Pt 0 from Hsp 1000 Pt.
- Figure 8 is an image showing (A) TEM of Hsp 250 Pt stained with 2% uranyl acetate.
- B Histogram of Pt particle diameters in Hsp 250 Pt. Scale bar) 20 nm.
- Figure 9 is a schematic presentation of the light-mediated H 2 production from Pt- Hsp.
- Methyl viologen (MV 2+ ) is used as an electron-transfer mediator between the Ru(bpy) 3 2+ photocatalyst and the Pt-Hsp responsible for H? production.
- Figure 10 is a graph showing H 2 production from Pt-Hsp in 0.2 mM Ru(bpy) 3 2+ , 0.5 mM methyl viologen, 200 mM EDTA, and 500 mM acetate pH 5.0: A , 1000 Pt/Hsp 5.1 x 10 "10 mol Pt; ⁇ , 250 Pt/Hsp 8.2 x 10 "10 mol Pt.
- the present invention is related to enzymatic H 2 formation, photocatalytic nanomaterials, and electro/photo-chromic polymer gel technology.
- the invention provides systems that substantially increase the efficiency with which H 2 can be produced from very simple feedstocks, namely visible light and simple organic acids (such as acetate - vinegar).
- simple organic acids such as acetate - vinegar.
- the inventors have demonstrated that using simple organic acids, visible light, and a photocatalyst, one can generate enough reducing equivalents to initiate activity of the hydrogenase enzyme and produce H 2 .
- hydro genase enzyme is immobilized and encapsulated into a polymer gel matrix and the resulting enzyme gel pellets are incubated with an electron donor such as dithionite and an electron transfer mediator such as methyl viologen to generate H 2 .
- an electron donor such as dithionite
- an electron transfer mediator such as methyl viologen
- the present invention is directed to the use of novel protein cages or nanoparticles as hydrogenase mimics " to produce hydrogen gas.
- the nanoparticles which comprise both a protein "shell” and a “core”, can be mixed together to form novel compositions of either complete nanoparticle or core mixtures.
- the shells can be loaded to form the complete nanoparticles with any number of different materials, including organic, inorganic and metallorganic materials, and mixtures thereof. Particularly preferred embodiments utilize metal catalyst such as platinum, to allow for efficient reduction of protons.
- the shells are proteinaceous, they can be altered to alter any number of physical or chemical properties by a variety of methods, including but not limited to covalent and non-covalent derivatization as well as recombinant methods.
- platinum is known for its high cost and limited supply. To maximize the use of this catalyst, it is necessary to explore ways of maximizing the catalytic efficiency of Pt on a per atom basis in order to develop economically feasible catalysts (Spiegel et al. 2004). In a particle based approach toward developing a Pt catalyst, it is necessary to minimize the diameter of the particle and thus increase the surface area ⁇ i.e., the number of exposed Pt atoms per particle). A number of different synthetic approaches have been used to synthesize platinum nanoparticles with different passivating layers (Brugger et al. 1981; Chen et al. 2000; Chen et al. 1999; Eldund et al.
- the passivating layer generally interferes with the exposed Pt atoms and reduces efficiency (Brugger et al. 1981).
- the inventors have employed a protein cage as a synthetic platform which, unlike a passivating layer, does not coat the entire surface of the nanoparticles but still isolates the particle in solution and prevents aggregation.
- Protein cage architectures have been used as biotemplates to create interfaces between proteins and metals (Allen et al., 2003; Flenniken et al. 2003). Cage-like architectures have previously been shown to act as a molecular container for the encapsulation of both organic and inorganic materials (Flenniken et al. 2003; McMillan et al. 2002). Protein cage architectures are self-assembled from a limited number of protein subunits to create well- defined, container-like morphologies in which the interior and exterior surfaces can be chemically distinct (Douglas and Young, 1998; Flenniken et al. 2003).
- TMOS tetramethoxysilane
- HCl tetrahydroxysilane
- Addition of the buffered (pH 8.0) protein solution (1 :1 v:v) initiates condensation forming the Si-O-Si network.
- Sol-gel pellets were cast from this mixture in Teflon wells or directly in reaction vials.
- the purified hydro genase from Clostridium pasteurianiim is a highly efficient catalyst for the reduction of H + to form H 2 .
- the long-term stability of this enzyme is significantly enhanced by modification of the protein through attachment of a thin polymer coating to the exterior surface of the protein or through encapsulation in polyelectrolyte multilayers. Additionally, the enzyme is immobilized within a 3-D cross-linked poly- viologen gel matrix for enhanced electron transfer efficiency.
- the efficient H 2 production from sunlight is accessed by controlling the amount of light and directly analyzing the amount of H 2 produced as a function of hydrogenase, photocatalyst, redox mediator, and electron donor.
- a Xe arc lamp which mimics the solar spectrum, has been utilized as a light source for these studies.
- the rate of hydrogen production can be measured directly in enzymatic assay as it has been previously described.
- the rate of H 2 is measured under conditions where mass transport of redox partners is minimized in the formulation of the composite materials described in detail in the Examples.
- Hydro genase and O? inhibition Incorporation of the hydrogenase into an electroactive polymer gel allows creation of a material having a core-shell structure.
- the outer layer may be incorporate with a photocatalyst, a redox mediator (viologen) and an O 2 reactive Cu colloid generated by photolysis of the catalyst. Cu is commonly used as an O 2 scavenger and the high surface area of the shell makes this very attractive for this purpose.
- the outer layer may act as an O 2 scrubbing layer to protect the hydrogenase present within the inner layer.
- the inner layer may comprise the photocatalyst, the hydrogenase, redox mediators, and electron donors. This engineered approach may significantly enhance the overall stability of the hydrogenase towards O 2 .
- Encapsulation of purified active hydrogenases in tetramethyl ortho silicate derived sol-gels has been demonstrated.
- the inventors have shown that a high percentage of the overall hydrogenase activity of both hydrogen oxidation and proton reduction is retained when these enzymes are embedded in these porous silica oxide polymeric gels.
- the activity of encapsulated hydrogenases from Clostridium pasterianum, Larnprobacter modestogalophilus, and Thiocapsa roseopersicina can be immobilized with an apparent activity at least 65-70% of that of the enzyme in solution measured in the reaction of hydrogen evolution.
- Encapsulated hydrogenases show some enhanced stability under storage and increased temperature.
- the present invention provides an immobilized hydrogenase system that consists of using various synthetic polymers to encapsulate molecules of hydrogenase.
- Various methods of encapsulation results in increased stability of the enzyme.
- Other factors with respect to optimization of the polymer matrix in which the hydrogenase enzyme are embedded are 1) the ability to dope the polymers with various electron transfer agents/mediators and 2) permeability of the polymer to substrates and products of the reaction.
- the following hydrogen producing enzymes have been successfully encapsulated: 1) Fe-only hydrogenase, 2) NiFe bidirectional hydrogenase, and 3) Alkaline phosphatase (oxidation of phosphate coupled to hydrogen production). Immobilization within these porous polymers allows for high-throughput heterogeneous catalysis.
- the immobilized catalyst systems allow reducing potential to be obtained through chemical or electrical means.
- the doping of the three-dimensional catalyst with electron transfer agents/mediators allows the external source of reducing power to be applied at the surface of the three-dimensional immobilized catalyst system.
- the present invention further provides a method of controllably expressing heterologous hydragenases in host cells.
- Controlled heterologous expression of hydrogenase from Shewanella oneldensis has been achieved in the host E. coil. This was accomplished by the simultaneous expression of hydrogenase structural genes and putative accessory gene products involved in hydrogenase maturation. Maximal hydrogenase expression may be achieved by optimization of the current system and by substitution of hydrogenase genes from various sources.
- the controlled expression allows genetic engineering of hydrogenase enzymes for enhancing stability, catalytic activity, and derivatization for the construction of composite materials. Photocatalytic H 2 generation
- the present invention further includes a method of utilizing photocatalyst in the process of generating hydrogen gas.
- the addition of photocatalysts adds an additional element of control to the system and potentially allows the use of lower potential electron transfer agents/mediators as a source of reducing equivalents.
- the catalyst systems operates through the application of either an electrical or chemical oxidation/reduction potential across the catalyst itself. Key components of the photocatalysts and their specific synthesis include:
- the present invention further provides a method of synthesizing nanoparticles with controlled size and composition.
- a biomimetic approach has been adopted to systematically alter the " composition of the metal oxide based nanomaterials to tune the efficiency of the photo-redox process.
- a range of protein encapsulated nanomaterials have been generated to evaluate the effect of composition of the effectiveness of MV generation.
- These materials include, but not limited to, Fe 2 O 3 , Fe 3 O 4 , Mn 2 O 3 , Mn 3 O 4 , Co 2 O 3 , Co 3 O 4 , TiO 2 ⁇ nH 2 O as well Fe- and Co- based materials doped with varying amounts of Ni(II), ZnSe, CdSe, CdS, ZnS, and MoS 2 . These materials have all been synthesized and structurally characterized.
- the present invention employs O 2 scavenger in the construction of Nanoparticles.
- Cu(O) which are highly O 2 reactive and can act as scavengers of O 2 may be encapsulated within protein cage architectures to protect the activity of hydrogenase (or other) redox active enzyme.
- a hydrogenase protein cage containing copper oxide may have several advantages.
- Cu acts as an in situ O 2 scavenging system and the high surface area of the nanoparticles makes this very attractive for the purpose.
- the reducing equivalents generated by the photoreduction OfMV + can be used to drive the turnover of the hydro genase system. The reduced MV + is not able to reduce Cu(II) to Cu(O) so these two products of the photoreduction are naturally independent of each other.
- the present invention provides a method of using protein case architecture as a platform for light harvesting molecules.
- the protein cage architectures of CCMV (and other viruses), ferritin (and ferritin-like proteins), small heat shock proteins, Dps proteins can be used as a multivalent templates for attachment of light harvesting molecules, which can be used to drive the photochemical reduction of electron transfer mediators (like methyl viologen).
- These include molecules such as Ru(II)bipyridine and Ru(II)phenanthroline which can be attached to the cages in a site specific manner.
- the reduced methyl viologen can be generated from the oxidized methyl viologen (MV) through the photochemical oxidation of organic species (EDTA, for example) with Ru(bpy) 3 2+ as the catalyst.
- EDTA organic species
- Ru(bpy) 3 2+ as the catalyst.
- light harvesting chromophores can be directly attached to redox active enzymes, such as hydrogenase, and potentially eliminate mass transport limitations and the need for electron transfer mediators such as methyl viologen.
- the present invention further provides a composition comprising a protein cage where catalyst nanoparticles are encapsulated.
- the inventors have demonstrated that nanoparticles of Pt can be efficiently encapsulated within the protein cage architectures (CCMV, ferritin, Hsp, Dps). These particles are size and shape constrained by the protein cage, giving rise to Pt colloids with very high relative surface areas, which yields high Ha formation through reduction of H + .
- the required reducing equivalents for this reaction can be supplied by reduced methyl viologen (MV).
- MV reduced methyl viologen
- the reduced viologen can be generated chemically by the oxidation of Zn (as Hg/Zn amalgam) in the presence of EDTA.
- H 2 generation maybe optimized through investigation of the Pt particle size dependence, nature of the protein cage architecture ⁇ i.e., diffusional access of the reduced viologen to the Pt nanoparticle), inhibiting catalyst poisoning for longevity, composition of the nanoparticle catalyst (e.g., Pd, CoPt, FePt), and the nature of the photocatalyst couple.
- the nanoparticle catalyst e.g., Pd, CoPt, FePt
- Synthesis of nanoparticles of different composition and alloy particles in particular may take advantage of the inventor's success in incorporating small peptides (derived from phage-display) onto the inside of the protein cage architectures. These peptides have been shown to direct the nucleation and particle growth of a particular inorganic solid and are also able to direct polymorph selection. Thus, the synthesis of a number of inorganic phases can be directed to screen for an optimal balance of long-term catalyst stability and activity in the reduction of H + to form H 2 .
- Pt particles encapsulated within the protein cage as disclosed herein serve as synthetic hydrogenase mimics.
- Such a system allows the incorporation of the best characteristics of colloidal catalysts with biological catalysts into a synthetic material. While both colloidal catalysts and biological catalysts have their own limitations (sensitivity to oxygen, poisoning, costs, and reaction conditions and longevity), a combination of these two types of catalyst circumvents these limitations.
- the present invention further includes reductants for reduced methyl viologen (and other) mediator formation.
- Organics such as ethyl enediamine tetraacetic acid, tartrate, citrate, acetate, ethanol (and other alcohols).
- Inorganics such as hydroxylamine, sulfite, thiosulfate, dithionite, and Zn can all be used.
- Sulfite SO 3 2"
- SO 2 + H 2 O- > HSO 3 " The oxidation of sulfite results in the formation of sulfate (SO 4 2" ).
- utilizing sulfite as a reductant also overcomes the problem of CO 2 generation caused by oxidation of organic species.
- the present invention further provides a method of facilitating electron transfer from redox protein to electrode.
- the nanoscopic confinement of redox active proteins in silica- derived sol-gel materials requires mediators, such as methyl viologen, to facilitate electron transfer with the protein.
- mediators such as methyl viologen
- the porous nature of these gels provides access to the encapsulated protein.
- Materials that facilitate direct electron transfer between an electrode surface and redox centers of hydrogenase and other redox active proteins will eliminate the catalytic dependence on chemical reductants.
- these novel materials will facilitate the flow of electrons from the encapsulated enzyme to an electrode during enzymatic ally catalyzed generation and oxidation of H-2 (g).
- the materials are derived from electroactive matrixes.
- a variety of bioelectronic glasses have been reported, including Sn- doped silica [SiVSiO 2 ], V 2 O 5 , MoO 3 , and MnO 2 .
- Hydrogenase can be coupled to the enzyme sulfite oxidase either 1) in a freely diffusing solution based system 2) by covalent attachment (cross-linking of sulfite oxidase and hydrogenase or 3) by the incorporation of both components in an electroactive porous gel.
- the reducing equivalents derived from the enzymatic oxidation of sulfite to sulfate can be directed to reduction of protons by hydrogenase.
- the oxidation of sulfite results in the formation of sulfate (SO 4 2" ).
- utilizing sulfite as a reductant also overcomes the problem of CO 2 generation caused by oxidation of organic species.
- Coupling photocatalysts to hydro genase Hydrogenase enzymes is coupled to photocataysts (including nanoparticle photocatalysts) in the development of heterogenous catalysts that can harness light energy to produce hydrogen from abundant electron donor sources such as sulfite, organic acids, or perhaps ethanol. Coupled systems can work in either aqueous solution or in immobilized gel.
- the components of the composite materials may be immobilized in electroactive gels (silica oxide or other polymers, for example, polyviologen).
- electroactive gels silicon oxide or other polymers, for example, polyviologen.
- the addition of oxygen consuming catalytic nanoparticles such as Cu(O) serves to protect the oxygen sensitive hydrogenases from oxygen inactivation.
- Example 1 Encapsulation of Hydrogenases in Polymer Gel This example is focused specifically on the hydrogen production activity of H 2 ase: sol- gel materials. Hydrogenases are bi-directional enzymes which also catalyze the oxidation of hydrogen. H 2 ase: sol-gel pellets were assayed for hydrogen oxidation activity by placing the pellets in buffered (pH 8.0) solution under a head pressure of hydrogen. Electron flow was monitored by the reduction of methyl viologen.
- H 2 ase sol-gel pellets with either the NiFe (Lamprobacter modestogalophilus (Lm) and Thiocapsa roseopersicina (Tr)) or Fe-only (Clostridium pasteurianum (CpI)) forms of H 2 ase retain approximately 60-70% of the hydrogen evolution specific activity observed in solution (Table 1) (Isolation of hydrogenases: (a) L. modestogalophilus: Zadvorny, O. A.; Zorin, N. A.; Gogotov, I. N.; Gorlenko, V. M. Biochemistry (Mosc) 2004, (5.9,164-169. (b) T. roseopersicina: Sherman, M. B.; Orlova, E.
- T Thhee aaccttiivviittyy mmeeaassure at 25 0 C is indicated in nmol/min/mg protein. The values represent average rate over a four-hour period.
- Example 2 Synthesis of Pt Nanoparticles Encapsulated within the Hsp Cage This example describes the synthesis of Pt nanoparticles encapsulated within the Hsp cage.
- the self-assembled cage-like architecture of the small heat shock protein (Hsp) from Methano co ecus j annas chii has been used to encapsulate metal clusters with a defined spatial arrangement (Flenniken et al. 2003).
- Hsp assembles from 24 subunits into a 12 nm cage defining a 6.5 nm interior cavity with pores through the cage architecture, by which molecules can shuttle between the inside and outside environment (Figure 5) (Kim et al. 1998).
- the Pt-Hsp protein cage composites are highly active artificial catalysts able to reduce H + to form H 2 at rates comparable to the highly efficient hydrogenase enzymes.
- reduced methyl viologen (MV ) was used as a source of reducing equivalents to drive the reaction.
- visible light and a cocatalyst (Ru(bpy) 3 2+ ) have been used to generate MV + through oxidation of simple organics such as EDTA (Brugger et al. 1981; Jiang et al. 2004) ( Figure 9).
- the solution was illuminated at 25 0 C with a 150 W Xe arc lamp equipped with an IR filter and a UV cutoff filter ( ⁇ 360 nm).
- the Pt-Hsp (0.51 ⁇ M) was illuminated in the presence of MV 2+ (0.5 mM), Ru(b ⁇ y) 3 2+ (0.2 mM), and EDTA (200 mM) at pH 5.0, and the resulting H 2 was quantified by gas chromatography.
- the initial rate of H 2 formation was 4.47 x 10 3 H 2 /s ((394 H 2 Zs) for a loading factor of 1000 Pt per Hsp and 7.63 x 10 2 H 2 /s ((405 H 2 /s) for a loading factor of 250 ( Figure 6). These rates are comparable to those reported for hydogenase enzymes (4 x 10 3 to 9 x 10 3 H2/s per protein molecule) (Adams et al. 1990).
- the initial rates for Pt-Hsp with 1000 Pt/ cage are 268 H 2 /Pt/min, which is significantly better than reported literature values (20 H 2 /Pt/min (Brugger et al. 1981 ), 16 H 2 /Pt/min (Keller et al. 1980), and 6.5 H 2 /Pt/min (Song et al. 2004), where comparisons are possible.
- initial H 2 production rates for Pt- Hsp are approximately 20-fold greater than those obtained for the Pt particles produced in protein-free control reactions.
- the long-term stability of the coupled photochemical reaction to produce H 2 has not been optimized, and a significant slowing down of the reaction is observed after the first 20 min (Figure 10).
- the H 2 production decay may be mainly due to the degradation of the photocatalyst Ru(bpy) 3 2+ , and the electron mediator (MV 2+ ), which is subject to Pt-catalyzed hydrogenation (Keller et al. 1980).
- the artificial Pt-Hsp systems are not sensitive to O 2 and show no significant inhibition of H 2 production by CO but are poisoned by thiols.
- the Pt- Hsp catalyzed reaction was driven by the presence of the reduced viologen (MV + ).
- the MV + could be generated either by the photoreduction described above or by using the Jones redactor (Harris et al. 1999) (Zn amalgam), which yielded rates for H 2 production approximately 40% slower than the coupled photoreduction reactions.
- the Pt-Hsp is able to catalyze the reverse reaction (H 2 ⁇ 2H + + 2e " ) as monitored by the in situ reduction and bleaching of methylene blue (Seeffeldt et al. 1989).
- the Pt-Hsp construct is remarkably stable and can be heated to 85 0 C without precipitation of the composite or loss of the catalytic activity.
- a well-defined thermally stable protein cage architecture has been used to generate an artificial hydro genase having many of the features common to those biological catalysts, small metal clusters in a spatially selective manner have been introduced to the interior of the cage-like structure of Hsp that act as active sites for the reduction of H + to form H 2 .
- the specific activities of these artificial enzymes are comparable to known hydrogenase enzymes and significantly better than previously described Pt nanoparticles.
- the protein cage architecture of Hsp acts to maintain the integrity of the small clusters, preventing agglomeration, and controlling access to these "active sites”.
- the Pt-Hsp composite is stable up to 85 0 C illustrating the utility of using protein architectures for the design and implementation of functional nanomaterials.
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US20100258446A1 (en) * | 2009-04-03 | 2010-10-14 | Board Of Regents Of The Nevada System Of Higher Education, On Behalf Of The University Of Nevada | Systems including nanotubular arrays for converting carbon dioxide to an organic compound |
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EP1902130A4 (en) | 2009-12-02 |
AU2006336421A1 (en) | 2007-08-02 |
CA2608870A1 (en) | 2007-08-02 |
WO2007086918A3 (en) | 2009-04-23 |
JP2008539786A (en) | 2008-11-20 |
US20080302669A1 (en) | 2008-12-11 |
CN101512003A (en) | 2009-08-19 |
WO2007086918A2 (en) | 2007-08-02 |
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