Kyushu University Academic Staff Educational and Research Activities Database
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Ki-Seok Yoon Last modified date:2020.07.26



Undergraduate School
Other Organization


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Homepage
https://kyushu-u.pure.elsevier.com/en/persons/ki-suk-yoon
 Reseacher Profiling Tool Kyushu University Pure
Phone
092-802-6688
Fax
092-802-6688
Academic Degree
Ph.D. (The University of Tokyo)
Country of degree conferring institution (Overseas)
Yes
Field of Specialization
Biotechnology, Applied Microbiology, Enzyme Technology, Biochemistry
Total Priod of education and research career in the foreign country
05years06months
Research
Research Interests
  • Development of novel biocatalysts involved in H2 activation, CO2 conversion, O2 activation, N2 fixation, and water-splitting reaction
    keyword : hydrogenase, CO2 fixing enzyme, photosynthetic water-oxidation, N2 fixation
    2013.02~2027.03.
Academic Activities
Papers
1. Ogo, Seiji; Kishima, Takahiro; Yatabe, Takeshi; Miyazawa, Keishi; Yamasaki, Ryunosuke; Matsumoto, Takahiro; Ando, Tatsuya; Kikkawa, Mitsuhiro; Isegawa, Miho; Yoon, Ki-Seok; Hayami, Shinya, [NiFe], [FeFe], and [Fe] Hydrogenase Models from Isomers, Sci. Adv. , 6, eaaz8181, 2020.06, The study of hydrogenase enzymes (H2ases) is necessary because of their importance to a future hydrogen energy
economy. These enzymes come in three distinct classes: [NiFe] H2ases, which have a propensity toward H2 oxidation;
[FeFe] H2ases, which have a propensity toward H2 evolution; and [Fe] H2ases, which catalyze H− transfer. Modeling
these enzymes has so far treated them as different species, which is understandable given the different cores and
ligand sets of the natural molecules. Here, we demonstrate, using x-ray analysis and nuclear magnetic resonance,
infrared, Mössbauer spectroscopies, and electrochemical measurement, that the catalytic properties of all three
enzymes can be mimicked with only three isomers of the same NiFe complex..