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• W1994191330 endingPage "4953" @default.
• W1994191330 startingPage "4949" @default.
• W1994191330 abstract "Irradiation of Agaricus bisporus tyrosinase in the presence of citrate at pH 5.6 with 300-420-nm light results in a loss of both catecholase activity and cresolase activity. The light-sensitive species appears to be an enzyme-citrate complex, most likely involving coordination of citrate to the active site copper. One copper ion from each binuclear active site can be removed from the inactivated enzyme, resulting in the formation of a met apo derivative. The electron spin resonance spectrum of met apo tyrosinase resembles that of met apo hemocyanin and half-met Neurospora tyrosinase. It is consistent with a distorted square-planar geometry around the copper and with either nitrogen or nitrogen and oxygen ligands. Amino acid analysis indicates that four histidines on the heavy subunit are destroyed during the inactivation process. Some or all of these histidines may serve as ligands to the copper ion which becomes labile after inactivation. Photoinactivation results in decarboxylation of citrate and does not require the presence of oxygen. The reaction may involve generation of a free radical from the citrate which then attacks nearby histidine residues." @default.
• W1994191330 created "2016-06-24" @default.
• W1994191330 creator A5051200255 @default.
• W1994191330 creator A5076599103 @default.
• W1994191330 date "1983-10-11" @default.
• W1994191330 modified "2023-10-10" @default.
• W1994191330 title "Photoinactivation of Agaricus bisporus tyrosinase: modification of the binuclear copper site" @default.
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• W1994191330 doi "https://doi.org/10.1021/bi00290a011" @default.
• W1994191330 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6416292" @default.
• W1994191330 hasPublicationYear "1983" @default.
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