Year: 1978
Type: article
Abstract: A mechanism was proposed which was consistent with the data obtained from the physical-chemical study and kinetic determinations.Oxygen binds to the copper dimers which are in the univalent state with the formation of peroxo-ion and 2 Cu(II).Hydrogen peroxide is released upon donation of protons from groups located on the protein.Glucose binds to the enzyme next, reducing the pairs of copper (II) to pairs of Cu (I) as was suggested by the diminished EPR signal shown under these conditions.The protons are replaced on the protein with D-glucono-5-lactone formation, completing the cycle.
Author: Daniel Kerschensteiner
Language: English
Subfield: Inorganic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W2807362416