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Bioinorganic Chemistry Lab
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A lab that investigates the active sites of metalloenzymes using model complexes and structural analysis.

AboutAbout the lab
Unraveling how metalloenzymes work through the lens of chemistry.
The Bioinorganic Chemistry Lab (Funahashi Lab) aims to investigate the structures and properties of the active sites of metalloenzymes and to elucidate chemically the reactions that take place in living organisms.
The research proceeds along two approaches, model synthesis using coordination chemistry and X-ray structure analysis and spectroscopic measurements of proteins, with the findings from each fed back to the other.
Another goal is to create new complex molecules and reaction systems inspired by the structures and reactions of metalloenzymes.
Lab visits are accepted at any time, whether you are from inside or outside the university.
Key terms
- Metalloenzyme
- A protein that contains a metal and acts as a catalyst for chemical reactions in living organisms. The site of the reaction is the metal active site.
- Complex
- A compound formed by molecules or ions binding around a metal. The lab uses it to make molecules modeled on the active sites of metalloenzymes.
- X-ray structure analysis
- A method of shining X-rays on a crystal of a protein or other substance to determine the three-dimensional structure of the molecule.
ResearchResearch themes
This lab aims to understand the structures and properties of the active sites of metalloenzymes and thereby chemically elucidate reactions in living organisms, and to build new complex molecules and reaction systems inspired by metalloenzymes. The research proceeds through two approaches: model synthesis making full use of coordination chemistry, and X-ray structure analysis and spectroscopic measurements of proteins.
*Illustrative imageOxygen activation by dinuclear copper enzymes
The lab studies how tyrosinase, an enzyme with a dinuclear copper center (Type III copper), uses oxygen to oxidize substrates. The aim is to reproduce with model compounds the reaction intermediate to which oxygen is bound, and to clarify the reaction mechanism.
*Illustrative imageModel studies of oxygen reduction and evolution
Focusing on oxygen reduction by multicopper oxidases and oxygen evolution by the manganese-calcium cluster in photosynthesis, the lab synthesizes and studies model compounds. For the former, the aim is to clarify the reaction mechanism and artificially reproduce the function; for the latter, to clarify the mechanism by which oxygen is evolved from water.
MembersFaculty
The Funahashi Lab's members consist of faculty members, a visiting associate professor, doctoral, master's, and undergraduate students, and secretaries.As of 2026
- ProfessorYasuhiro Funahashi
- LecturerMasaki Nojiri
VoicesStudent voices
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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: “Crystal structure of human hemoglobin in the oxy form” PDB code 2DN1 1.25 a resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. Park, S.-Y., Yokoyama, T., Shibayama, N., Shiro, Y., Tame, J.R. (2006) J Mol Biol 360: 690-701 DOI: 10.1016/j.jmb. Image created using JSmol (Javascript) / CC0 (cropped)
- Oxygen activation by dinuclear copper enzymes: “Consurf tyrosinase protein” Bhatchhetrbb / CC BY-SA 4.0 (cropped)
- Model studies of oxygen reduction and evolution: “Photosystem-II 2AXT” Neveu,Curtis (C31004) / CC BY-SA 3.0 (cropped)
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- Related lab (高分子反応化学研究室): “Polypropylene Pellets - DPLA - f7c2fa29d14525ce21219452f4a1a316” Quantum Chemical Corporation / CC BY 4.0 (cropped)
- Related lab (錯体化学研究室): “Fe(C2O4)(H2O)2-chain-from-xtal-2008-CM-3D-balls” Ben Mills / Public domain (cropped)
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