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Biofunctional Chemistry Lab
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A lab that learns from how metalloenzymes work to create oxidation catalysts.
AboutAbout the lab
Learning from enzymes to create new molecules.
The Biofunctional Chemistry Lab studies how metalloenzymes with transition metals at their active sites work, with the aim of developing new oxidation catalysts.
The lab builds model complexes that artificially mimic enzyme active sites, and investigates their structures and reactivity using methods such as spectroscopy and electrochemistry.
It also works with actual proteins (enzymes), using genetic engineering techniques to create artificial metalloenzymes.
The lab's website is published under the name "Ito Lab."
Key terms
- Metalloenzyme
- An enzyme that has a metal ion, such as iron or copper, at its active site. Metalloenzymes are involved in oxygen transport and the oxidation of substances.
- Active site
- The part of an enzyme where the reaction actually takes place.
- Model complex
- A metal-containing molecule made to artificially mimic the active site of an enzyme.
ResearchResearch themes
Metalloenzymes oxidize substances using oxygen from the air or water as the oxygen source, without producing harmful by-products. This lab clarifies the structures, properties, and reactivity of the reactive species of metalloenzymes, and aims to develop new molecular catalysts that apply the strategies of metalloenzymes.
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MembersFaculty
The members of the Biofunctional Chemistry Lab consist of faculty, graduate students, undergraduate students, and administrative assistants.As of 2025
- Associate ProfessorHideki Sugimoto
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Report an errorAbout the images
The top and research theme images are illustrative and were not taken at the lab. They are cropped from Wikimedia Commons images. Cropped CC BY-SA images are provided under the same CC BY-SA license as the original (version shown on each line).
- Top image: “Picture of Active Site 1Y79” PDB code 1Y79 Crystal Structure of the E.coli Dipeptidyl Carboxypeptidase Dcp: Further Indication of a Ligand-dependant Hinge Movement Mechanism Comellas-Bigler, M., Lang, R., Bode, W., Maskos, K. (2005) J Mol Biol 349: 99-112 DOI: 10.1016/j.jmb. Image created using JSmol (javascript) and CCP4MG / CC0 (cropped)
- Developing oxidation catalysts inspired by metalloenzymes: “Azurin copper binding domain” Jmsliu / CC BY-SA 4.0 (cropped)
- Related lab (精密資源化学領域): “Kristallisierschale” MediaLab TH Köln / CC BY-SA 4.0 (cropped)
- Related lab (構造有機化学領域): “Chemistry Experiment 3D” TeWeBs / CC BY-SA 4.0 (cropped)
- Related lab (分子微生物学領域
[生物工学国際交流センター] ): “Hot spring in Yellowstone” Jon Sullivan / Public domain (cropped) - Related lab (先進無機材料化学領域): “Dr Thaddeus (Tadj) Asel focuses on the growth of oxide semiconductor materials such as Gallium Oxide to address the need for smaller and higher power electronics (8380286)” U.S. Air Force AFRL by Keith C Lewis / Public domain (cropped)
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