Kyoto University · Engineering
Professor Keisei Sowa's research lab specializes in the structural and electrochemical characterization of redox enzymes, particularly those capable of direct electron transfer (DET) with electrodes. The lab focuses on understanding the 3D structures, electron transfer pathways, and electrode-interaction mechanisms of dehydrogenases such as formate dehydrogenase and fructose dehydrogenase, with applications in bioelectrocatalysis, biosensors, and biofuel cells. By integrating structural biology (including cryo-EM), bioelectrochemistry, and protein engineering, the lab aims to unlock the design principles of efficient, mediator-free biocatalytic systems.
Figures are computed from collected data and may differ slightly.
Tungsten-containing formate dehydrogenase from <i>Methylorubrum extroquens</i> AM1 (FoDH1)-a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD<sup>+</sup>)/NADH redox couples-was investigated using structural biology and bioelectrochemistry. FoDH1 is reported to be an enzyme that can realize "direct electron transfer (DET)-type bioelectrocatalysis." However, its 3-D structure, electrode-active sites, and electron transfer (ET) pathways
Flavin adenine dinucleotide-dependent d-fructose dehydrogenase (FDH) from Gluconobacter japonicus NBRC3260, a membrane-bound heterotrimeric flavohemoprotein capable of direct electron transfer (DET)-type bioelectrocatalysis, was investigated from the perspective of structural biology, bioelectrochemistry, and protein engineering. DET-type reactions offer several benefits in biomimetics (e.g., biofuel cells, bioreactors, and biosensors) owing to their mediator-less configuration. FDH provides an
Among the various types of enzyme-based biosensors, sensors utilizing enzymes capable of direct electron transfer (DET) are recognized as the most ideal. However, only a limited number of redox enzymes are capable of DET with electrodes, that is, dehydrogenases harboring a subunit or domain that functions specifically to accept electrons from the redox cofactor of the catalytic site and transfer the electrons to the external electron acceptor. Such subunits or domains act as built-in mediators f
Direct electron transfer (DET)-type bioelectrocatalysis, in which enzymatic reactions proceed without the involvement of redox mediators, is a powerful approach for investigating intrinsic enzymatic features relevant to the development of advanced biomimetic systems.However, because numerous DET-capable enzymes are associated with cellular membranes, determining their full three-dimensional conformations is challenging when relying solely on conventional X-ray crystallography.The advent of cryo-
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