Yong Hwan Kim
UNIST
Bio
Dr. Yong Hwan Kim is a professor at the School of Energy and Chemical Engineering at UNIST (Ulsan National Institute of Science and Technology) in Korea. He began his academic career at Seoul National University, where he earned his bachelor’s, master’s, and Ph.D. degrees. After completing his Ph.D. in 1996, Dr. Kim spent four years in industry, working in R&D at the Samsung Advanced Institute of Technology and Samsung Engineering. He then transitioned to the National Lab (Korea Research Institute of Chemical Technology) as a principal scientist, where he focused on bridging biotechnology and chemical technology. Since 2015, his research has centered on fundamental studies of metalloenzymes, including heme peroxidases and enzymes containing nickel or tungsten that are involved in C1 conversion in academy. Dr. Kim also serves as the director of the Engineering Research Centre for Microplastics treatment (ERC) and the Dean of the College of Engineering at UNIST and member of the National Academy of Engineering of Korea.
Area(s) of Expertise
Title: Defining the Molecular Logic of MeFDH1: Tungsten-Pterin Cofactor Assembly and the Structural Basis of Viologen-Mediated Electron Transfer for CO2 reduction in large scale
Abstract:
Tungsten-dependent formate dehydrogenase 1 from Methylorubrum extorquens (MeFDH1) is a premier biocatalyst for reversible CO₂/formate interconversion, but scalable deployment demands control over both metallocofactor maturation and redox wiring to low-potential mediators. This presentation defines the molecular logic that creates the functional form of MeFDH1 from the cell to the reactor. We first delineate a dedicated tungsten–pterin (W-bis-MGD) assembly and delivery pathway, identifying the MoeA1 insertase and MobB scaffold as key determinants that enforce tungsten selectivity over molybdate and remove a major bottleneck in producing active holoenzyme. We then resolve the structural basis of viologen (ethyl viologen, EV) electron transfer, revealing a dual-interaction strategy: a primary FMN-centered binding mode and an FMN-independent “aromatic cage” (F232/F471/Y329) that positions EV near the proximal B1 Fe–S cluster to sustain CO₂ reduction when flavin occupancy is limiting. Finally, we translate these insights to process engineering, demonstrating MeFDH1 operation in a 10-L pilot reactor fed with live steel-mill off-gases to achieve molar-scale formate production. Together, these results deliver actionable design rules for improving assembly yields, reducing mediator requirements, and de-risking industrial CO₂-to-formate biomanufacturing.