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- W2078343857 abstract "1.|Copper-free stellacyanin, a blue copper protein from the latex of Rhus vernicifera, has been prepared by dialysis against CN− at pH 11 and the ability of recombination with copper to restore the native protein was tested by optical, electron paramagnetic resonance and fluorimetric methods. 2.|One sulfhydryl group per molecule of apoprotein was titrated with p-chloromercuribenzoate while native stellacyanin did not react at all. 3.|Addition of stoichiometric amounts of Cu2+ quenched the fluorescence of apoprotein to 30% of its value and produced a blue shift of 5 nm. One tryptophan out of the three present per molecule was found to be responsible for these changes. 4.|The same quenching effect was obtained with Hg2+ and Ag+. These ions also inhibited the recombination of Cu2+ with apostellacyanin. 5.|It is suggested that one sulfhydryl and one tryptophan at the copper site contribute to the unique features of the copper chromophore, as already shown in azurin." @default.
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- W2078343857 date "1972-07-01" @default.
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- W2078343857 title "Studies of the metal sites of copper proteins IV. Stellacyanin: Preparation of apoprotein and involvement of sulfhydryl and tryptophan in the copper chromophore" @default.
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- W2078343857 doi "https://doi.org/10.1016/0005-2795(72)90203-6" @default.
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