Emission spectra from copper proteins containing type-3 centres.
Aqueous solutions of copper-proteins containing type-3 centres (ceruloplasmin, tyrosinase, haemocyanin), excited within their absorption bands at 325-345 nm, show typical luminescence spectra. The emission bands peak at 415-445 nm and their decay time is no longer than 10 ns. A strong analogous fluorescence is obtained also by excitation of concentrated solutions of carboxylic acids and amino acids, which show again absorption bands around 330 nm. Such a fluorescence, although less intense, is also observed in copper(II) carboxylate solutions. In contrast, no fluorescence has been recorded in solutions of acetic anhydride and of polypeptides (valinomycin, gramicidin D), which do not have free carboxyl groups. We tentatively attribute this novel fluorescence in the investigated copper proteins to interactions between carboxyl groups of amino acids at, or near, the active site.
D000818:Animals; D001487:Basidiomycota; D004156:Catechol Oxidase; D002570:Ceruloplasmin; D003300:Copper / Q000032:analysis*; D006433:Hemocyanins; D006737:Horseshoe Crabs; D006801:Humans; D008163:Luminescent Measurements; D014442:Monophenol Monooxygenase; D013050:Spectrometry, Fluorescence
D003300:Copper; D006433:Hemocyanins; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase; D002570:Ceruloplasmin