FLUORESCENCE PROPERTIES OF NEUROSPORA TYROSINASE

被引:18
作者
BELTRAMINI, M [1 ]
LERCH, K [1 ]
机构
[1] UNIV ZURICH, INST BIOCHEM, CH-8028 ZURICH, SWITZERLAND
关键词
D O I
10.1042/bj2050173
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Some structural properties of Neurospora tyrosinase were studied by fluorescence spectroscopy. The emission spectra observed for oxy-, deoxy-, met- and apo-tyrosinase and the Co2+-substituted form are indicative of a protein containing buried tryptophan residues. By using acrylamide and iodide, part of the emission is quenched, indicating heterogeneity in the tryptophan environment. Upon binding of Cu2+ or Co2+ to apo-tyrosinase, a marked decrease of the tryptophan quantum yield is observed. A further decrease in emission intensity results from the binding of molecular O2 to the deoxy form. The fluorescent probe 8-anilinonaphthalene-1-sulfonate binds to tyrosinase only when the metal ions are removed. Reconstitution of apo-tyrosinase with Cu2+ completely displaces the probe, suggesting that 8-anilinonaphthalene-1-sulfonate binds to apo-tyrosinase at the active site. The fluorescence properties of Neurospora tyrosinase are compared with those of hemocyanin.
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页码:173 / 180
页数:8
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