Fluorescence Properties of Neurospora Tyrosinase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1982 Jul 1

PMID 6215031

Citations 1

Authors

M Beltramini

K Lerch

Affiliations

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Abstract

Some structural properties of Neurospora tyrosinase have been 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-sulphonate 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-sulphonate binds to apo-tyrosinase at the active site. The fluorescence properties of Neurospora tyrosinase are compared with those of haemocyanin.

Citing Articles

Neurospora tyrosinase: structural, spectroscopic and catalytic properties.

Lerch K Mol Cell Biochem. 1983; 52(2):125-38.

PMID: 6308414 DOI: 10.1007/BF00224921.

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