ISSN:
1432-1327
Keywords:
Key words Laccase
;
Copper protein
;
Type 2-depleted laccase
;
EPR spectroscopy
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract Understanding the structure and function of the three copper atoms in the dioxygen reduction site of the blue oxidases such as laccase has been a long standing challenge. In the case of a widely studied derivative, known as type 2-depleted laccase, the removal of one copper from the cluster abolishes the EPR signal of the so-called type 2 copper. However, the present studies of isotopically enriched protein from Polyporus versicolor show that the readily replaceable copper is not active in the low-temperature EPR spectrum of fungal laccase or its difluoride adduct. The same is true for the difluoride adduct of the tree enzyme. Thus, in type 2-depleted laccase the pattern of antiferromagnetic coupling is quite different from that of the native protein or the difluoride adduct.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s007750050303
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