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Applying Dynamic Strain on Thin Oxide Films Immobilized on a Pseudoelastic Nickel-Titanium Alloy

Direct alteration of material structure/function through strain is a growing area of research that has allowed for novel properties of materials to ...

National Renewable Energy Laboratory

Many envision a future where hydrogen is the centerpiece of a sustainable, carbon-free energy supply. For example, the energy in sunlight may be stored by splitting water into H2 and O2 using inorganic semiconductors and photoelectrochemical approaches or with artificial photosynthetic systems that seek to mimic the light absorption, energy transfer, electron transfer, and redox catalysis that occurs in green plants. Unfortunately, large scale deployment of artificial water-splitting technologies may be impeded by the need for the large amounts of precious metals required to catalyze the multielectron water-splitting reactions. Nature provides a variety of microbes that can activate the dihydrogen bond through the catalytic activity of [NiFe] and [FeFe] hydrogenases, and photobiological approaches to water splitting have been advanced. One may also consider a biohybrid approach; however, it is difficult to interface these sensitive, metalloenzymes to other materials and systems. Here we show that surfactant-suspended carbon single-walled nanotubes (SWNTs) spontaneously self-assemble with [FeFe] hydrogenases in solution to form catalytically active biohybrids. Photoluminescence excitation and Raman spectroscopy studies show that SWNTs act as molecular wires to make electrical contact to the biocatalytic region of hydrogenase. Hydrogenase mediates electron injection into nanotubes having appropriately positioned lowest occupied molecular orbital levels when the H2 partial pressure is varied. The hydrogenase is strongly attached to the SWNTs, so mass transport effects are eliminated and the absolute potential of the electronic levels of the nanotubes can be unambiguously measured. Our findings reveal new nanotube physics and represent the first example of "wiring-up" an hydrogenase with another nanoscale material. This latter advance offers a nonprecious metal route to the design of new biohybrid architectures and building blocks for hydrogen-related technologies.

Wiring-up hydrogenase with single-walled carbon nanotubes.

We report a Raman spectroscopy study of charge transfer interactions in complexes formed by single-walled carbon nanotubes (SWNTs) and [FeFe] hydrogenase I (CaHydI) from Clostridium acetobutylicum. The choice of Raman excitation wavelength and sample preparation conditions allows differences to be observed for complexes involving metallic (m) and semiconducting (s) species. Adsorbed CaHydI can reversibly inject electronic charge into the LUMOs of s-SWNTs, while charge can be injected and removed from m-SWNTs at lower potentials just above the Fermi energy. Time-dependent enzymatic assays demonstrated that the reduced and oxidized forms of CaHydI are deactivated by oxygen, but at rates that varied by an order of magnitude. The time evolution of the oxidative decay of the CaHydI activity reveals different time constants when complexed with m-SWNTs and s-SWNTs. The correlation of enzymatic assays with time-dependent Raman spectroscopy provides a novel method by which the charge transfer interactions may be investigated in the various SWNT-CaHydI complexes. Surprisingly, an oxidized form of CaHydI is apparently more resistant to oxygen deactivation when complexed to m-SWNTs rather than s-SWNTs.

Raman spectroscopy of charge transfer interactions between single wall carbon nanotubes and [FeFe] hydrogenase.

We studied the electrocatalytic activity of an [FeFe]-hydrogenase from Clostridium acetobutylicum (CaH2ase) immobilized on single-wall carbon nanotube (SWNT) networks. SWNT networks were prepared on carbon cloth by ultrasonic spraying of suspensions with predetermined ratios of metallic and semiconducting nanotubes. Current densities for both proton reduction and hydrogen oxidation electrocatalytic activities were at least 1 order of magnitude higher when hydrogenase was immobilized onto SWNT networks with high metallic tube (m-SWNT) content in comparison to hydrogenase supported on networks with low metallic tube content or when SWNTs were absent. We conclude that the increase in electrocatalytic activities in the presence of SWNTs was mainly due to the m-SWNT fraction and can be attributed to (i) substantial increases in the active electrode surface area, and (ii) improved electronic coupling between CaH2ase redox-active sites and the electrode surface.

High-performance hydrogen production and oxidation electrodes with hydrogenase supported on metallic single-wall carbon nanotube networks.

We report the ability to tune the catalytic activities for the hydrogen evolution reaction (HER) and oxygen evolution reaction (OER) by applying mechanical stress on a highly n-type doped rutile TiO films. We demonstrate through operando electrochemical experiments that the low HER activity of TiO can reversibly approach those of the state-of-the-art non-precious metal catalysts when the TiO is under tensile strain. At 3% tensile strain, the HER overpotential required to generate a current density of 1 mA/cm shifts anodically by 260 mV to give an onset potential of 125 mV, representing a drastic reduction in the kinetic overpotential. A similar albeit smaller cathodic shift in the OER overpotential is observed when tensile strain is applied to TiO. Results suggest that significant improvements in HER and OER activities with tensile strain are due to an increase in concentration of surface active sites and a decrease in kinetic and thermodynamics barriers along the reaction pathway(s). Our results highlight that strain applied to TiO by precisely controlled and incrementally increasing (i.e. dynamic) tensile stress is an effective tool for dynamically tuning the electrocatalytic properties of HER and OER electrocatalysts relative to their activities under static conditions.

Dynamic Tuning of a Thin Film Electrocatalyst by Tensile Strain.

Substrate channeling studies have frequently failed to provide conclusive results due to poor understanding of this subtle phenomenon. We analyzed the mechanism of NADH-channeling from D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-lactate Dehydrogenase (LDH) using enzymes from different cells. Enzyme kinetics studies showed that LDH activity with free NADH and GAPDH-NADH complex always take place in parallel. The channeling is observed only in assays that mimic cytosolic conditions where free NADH concentration is negligible and the GAPDH-NADH complex is dominant. Molecular dynamics and protein-protein interaction studies showed that LDH and GAPDH can form a leaky channeling complex only at the limiting NADH concentrations. Surface calculations showed that positive electric field between the NAD(H) binding sites on LDH and GAPDH tetramers can merge in the LDH-GAPDH complex. NAD(H)-channeling within the LDH-GAPDH complex can be an extension of NAD(H)-channeling within each tetramer. In the case of a transient LDH-(GAPDH-NADH) complex, the relative contribution from the channeled and the diffusive paths depends on the overlap between the off-rates for the LDH-(GAPDH-NADH) complex and the GAPDH-NADH complex. Molecular evolution or metabolic engineering protocols can exploit substrate channeling for metabolic flux control by fine-tuning substrate-binding affinity for the key enzymes in the competing reaction paths.

Article	Year
Wiring-up hydrogenase with single-walled carbon nanotubes. Nano letters\| PubMed ID: 17967044	2007
Raman spectroscopy of charge transfer interactions between single wall carbon nanotubes and [FeFe] hydrogenase. Dalton transactions (Cambridge, England : 2003)\| PubMed ID: 19082027	2008
High-performance hydrogen production and oxidation electrodes with hydrogenase supported on metallic single-wall carbon nanotube networks. Journal of the American Chemical Society\| PubMed ID: 21384925	2011
Dynamic Tuning of a Thin Film Electrocatalyst by Tensile Strain. Scientific reports\| PubMed ID: 31685891	2019
Substrate Channeling via a Transient Protein-Protein Complex: The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase. Scientific reports\| PubMed ID: 32591631	2020

Drazenka Svedruzic

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