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Bioinorganic Chemistry Lab
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A lab that investigates the active sites of metalloproteins through metal complexes and structural analysis.
AboutAbout the lab
Unraveling the active sites of metalloproteins through chemistry
The Bioinorganic Chemistry Lab aims to understand the structures and properties of the active centers of metalloenzymes and to elucidate chemically the chemical reactions that take place in living organisms.
Another goal is to create new metal complexes and reaction systems inspired by the structures of metalloenzymes and the reactions they carry out.
The lab approaches the metal active sites of metalloproteins in two ways: model synthesis using coordination chemistry, and X-ray structure analysis and spectroscopic measurements of proteins.
Lab visits are accepted at any time, from both within and outside the university.
Key terms
- Metal active site
- The part of a metalloprotein in which the metal is involved at the center of a chemical reaction
- Tyrosinase
- An enzyme with a dinuclear copper center. It introduces a hydroxyl group into tyrosine residues and produces the precursor of melanin pigment
- Complex
- A compound in which molecules or ions are bound to a metal
ResearchResearch themes
This lab aims to understand the structures and properties of the active centers of metalloenzymes and to elucidate chemically the chemical reactions that take place in living organisms. Another goal is to use the structures and reactions of metalloenzymes as clues to create new metal complexes and reaction systems.
*Illustrative imageOxygen Activation by Dicopper Enzymes
Hemocyanin, which carries oxygen in the blood of octopuses and squid, and tyrosinase, which produces the precursor of melanin pigment, both contain a dinuclear copper center. Using model compounds, the lab reproduces the reaction intermediates in which oxygen is bound and investigates the reaction mechanism of tyrosinase.
*Illustrative imageMechanisms of Oxygen Reduction and Oxygen Evolution
Using model compounds, the lab investigates how the trinuclear copper center of multicopper oxidases such as laccase reduces oxygen all the way to water. The lab also uses model compounds to study the manganese–calcium cluster that releases oxygen from water in photosynthesis.
MembersFaculty
The members of the Bioinorganic Chemistry Lab consist of faculty, a Visiting Associate Professor, doctoral, master's, and undergraduate students, and administrative staff.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: “Mo active site” Swiftie1999 / CC BY-SA 4.0 (cropped)
- Oxygen Activation by Dicopper Enzymes: “Hemocyanin Example” Jerry Kirkhart / CC BY 2.0 (cropped)
- Mechanisms of Oxygen Reduction and Oxygen Evolution: “Cu3Im8laccase” Smokefoot / Public domain (cropped)
- Related lab (Supramolecular Functional Chemistry Lab): “Antibody je2-gl” Je at uwo / CC0 (cropped)
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- Related lab (Macromolecular Structural Science Lab): “Flagellar Motor Assembly” PKS615 / CC BY 4.0 (cropped)
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