Roman Brunecky
NLR
Bio
Dr. Brunecky is a senior research scientist at NLR, with primary expertise in enzyme structure function relationships and enzyme material interfaces, best known for his work on cellulases and biomass degrading enzymes. His research spans enzyme expression, purification, and mechanistic characterization, with a long-standing focus on how enzyme orientation, confinement, and surface interactions govern activity and stability. More recently, this expertise has been applied to redox enzymes, including formate dehydrogenase (FDH), in the context of hybrid bio electrochemical and electro-to-microbial (E2M) systems. In this role, Dr. Brunecky brings a mechanistic, enzyme-centric perspective to the design of nanowire- and self-assembled monolayer based interfaces that enable controlled enzyme wiring and interpretable electrochemical behavior. His work emphasizes reproducibility and fundamental understanding of enzyme–interface interactions as a foundation for robust integration of biological catalysts with engineered materials.
Area(s) of Expertise
Title: Controlled Electrochemical Wiring of FDH via Nanowires and Self-Assembled Interfaces
This talk examines electrochemical coupling in formate dehydrogenase (FDH)–based bio electrochemical systems with emphasis on engineering electrode interfaces that enable controlled enzyme orientation and wiring. Earlier FDH electrochemistry work has largely relied on nonspecific adsorption or “drop-cast” enzyme layers on electrodes, limiting reproducibility and obscuring relationships between electrochemical signals and enzymatic function. In contrast, the current effort focuses on nanowire- and self-assembled monolayer (SAM)–based architectures designed to impose defined spatial organization and electron transfer pathways at the enzyme electrode interface.
This presentation summarizes our current project efforts and reports new measurements validate that key electrochemical features persist under controlled wiring conditions and are not artifacts of poorly defined enzyme attachment. These results provide an internally consistent and interpretable electrochemical baseline that has not previously been broadly disseminated.
Collectively, these results demonstrate the value of nanowires and SAMs as tools for disentangling orientation, proximity, and coupling effects in FDH electrochemistry. The emphasis is on mechanistic understanding of enzyme–electrode interfaces and system-level behavior, establishing a foundation for rational design of more robust and scalable FDH-driven bio electrochemical systems.