When your wounds heal and your liver detoxifies a poison such as histamine you ingested, you can thank the class of enzymes known as copper amine oxidases for their assistance. Identifying the exact positions of the smallest hydrogen atoms in these enzymes is challenging with commonly used technologies, but is critical to engineering improved enzymes that exhibit unusual yet useful biochemical reactivity.
"There are pH-dependence, conformational change, and radical intermediate stabilization questions of our enzyme that X-ray crystallography in itself cannot fully explain," explains Takeshi Murakawa, lead author of the study."Neutron crystallography is well-suited for answering these questions."
Conformational change of cofactor TPQ during the catalysis. TPQ undertakes a conformational change from off-Cu to on-Cu in a manner that generates a semiquinone radical intermediate. Credit: Takeshi Murakawa, Toshihide Okajima
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