Kyoto University · 공학
Keisei Sowa 교수의 연구실은 생물전기화학과 구조생물학을 융합한 연구를 중심으로, 이산화탄소와 포름산을 상호 변환할 수 있는 텅스텐 함유 포름산 탈수소효소(FoDH1)와 페리민산 함유 당 탈수소효소(FDH)를 중심으로 직접 전자 이송(DET) 메커니즘을 규명하고 있습니다. 특히, 전자 전달 경로, 전극 활성 부위, 그리고 단백질의 3차원 구조를 고해상도 구조 분석 기법(크리오전자현미경 등)을 통해 규명함으로써, 생체 모방 전기화학 장치(예: 생체연료전지, 생물센서)의 핵심 소재로 활용 가능한 효소를 개발하고자 합니다. 연구는 생물학적 촉매의 내재적 전자 이동 특성과 그 응용 가능성을 동시에 탐구하는 데 초점을 맞추고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
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-
