The utilization of CO2 to generate chemical fuels, such as formic acid, is a potentially beneficial route to balance carbon emissions and reduce dependence on fossil fuels. The development of efficient catalysts for CO2 hydrogenation is needed to implement this fuel generation. In the molecular catalyst design presented here, we covalently attached a rhodium complex, ([RhI(PNglyP)2]−, where PNglyP is defined as PEt2 –CH2–N(CH2CO2 –)–CH2–PEt2 ) to a protein scaffold, (lactococcal multidrug resistant regulator from Lactococcus lactis) to use the protein environment around the metal center to control substrate delivery and therefore enable and improve catalytic activity. The reactivities of the rhodium complex and the synthetic metalloenzyme were characterized by high-pressure operando NMR techniques. In solution, the rhodium complex alone is not a catalyst for CO2 hydrogenation. Incorporation of the rhodium complex into the protein scaffold resulted in a gain of function, turning on CO2 hydrogenation activity. The metalloenzyme displayed a turnover frequency of 0.38 ± 0.03 h–1 at 58 atm and 298 K and achieved an average turnover number of 14 ± 3. Proposed catalytic intermediates generated and characterized suggest that the protein scaffold enables catalysis by facilitating the interaction between CO2 and the hydride donor intermediate.

A facile surface-amide coupling method was examined to attach dye and catalyst molecules to silatrane-decorated NiO electrodes. Using this method, electrodes with a push-pull dye were assembled, and characterized by photoelectrochemistry and transient absorption spectroscopy. The dye-sensitized electrodes exhibited hole injection into NiO and good photoelectrochemical stability in water, highlighting the stability of the silatrane anchoring group and the amide linkage. The amide coupling protocol was further applied to electrodes that contain additional proton reduction nickel catalysts for use in photocathode architectures. Evidence for catalyst reduction was observed during photoelectrochemical measurements and via fs-transient absorption spectroscopy demonstrating the possibility for application in photocathodes.

A virtual reality (VR) session was introduced to an advanced inorganic chemistry class, a class available to junior and senior undergraduate students at the University of California, Los Angeles. The VR session helped the students to learn complicated aspects of metal coordination chemistry and molecular orbitals via an immersive three-dimensional experience.

Virtual reality is a powerful tool with the ability to immerse a user within a completely external environment. This immersion is particularly useful when visualizing and analyzing interactions between small organic molecules, molecular inorganic complexes, and biomolecular systems such as redox proteins and enzymes. A common tool used in the biomedical community to analyze such interactions is the Adaptive Poisson-Boltzmann Solver (APBS) software, which was developed to solve the equations of continuum electrostatics for large biomolecular assemblages. Numerous applications exist for using APBS in the biomedical community including analysis of protein ligand interactions and APBS has enjoyed widespread adoption throughout the biomedical community. Currently, typical use of the full APBS toolset is completed via the command line followed by visualization using a variety of two-dimensional external molecular visualization software. This process has inherent limitations: visualization of three-dimensional objects using a two-dimensional interface masks important information within the depth component. Herein, we have developed a single application, UnityMol-APBS, that provides a dual experience where users can utilize the full range of the APBS toolset, without the use of a command line interface, by use of a simple graphical user interface (GUI) for either a standard desktop or immersive virtual reality experience.