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9. The essential role of Glu-185 and Tyr-354 residues in the ferroxidase activity of Saccharomyces cerevisiae Fet3.

Author

Bonaccorsi di Patti MC, Felice MR, Camuti AP, Lania A, and Musci G

Subjects
Catalysis, Ceruloplasmin chemistry, Ceruloplasmin genetics, Glutamic Acid genetics, Glutamic Acid metabolism, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Tyrosine genetics, Tyrosine metabolism, Ceruloplasmin metabolism, Glutamic Acid physiology, Saccharomyces cerevisiae enzymology, Tyrosine physiology
Abstract

The structural determinants required for ferroxidase activity by the yeast multicopper oxidase Fet3 have been partially clarified by site-directed mutagenesis based on homology modeling. Glu-185 and Tyr-354 were substituted with Ala and Phe, respectively. Fet3 E185A retained ca. 5% residual ferroxidase catalytic efficiency, and almost 40% oxidase efficiency. On the other hand, Fet3 Y354F exhibited 50% residual efficiency as a ferroxidase and more than 70% as an oxidase. These results provide new insights in the mechanism of iron binding and oxidation by Fet3, establishing the essential role of Glu-185 and Tyr-354, and allowing to dissect ferroxidase from non-iron oxidase activity.

Published
2000
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