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Coordination environment and fluoride binding of type 2 copper in the blue copper oxidase ceruloplasmin

By John H. Dawson, David M. Dooley and Harry B. Gray

Abstract

The electron paramagnetic resonance (EPR) spectra of the blue copper oxidase ceruloplasmin [ferroxidase, iron(II):oxygen oxidoreductase, EC 1.16.3.1] and of a derivative having the type 1 (blue) copper centers reversibly bleached are reported. The EPR spectrum of bleached ceruloplasmin has a seven-line superhyperfine structure in the g[perpendicular] region that is attributed to the presence of three nitrogen-donor type 2 copper ligands. The EPR data suggest further that the type 2 copper in ceruloplasmin possesses a tetragonal coordination gometry. In the presence of varying amounts of fluoride, superhyperfine splitting patterns in the g[parallel] region of both ceruloplasmin derivatives indicate that a maximum of two fluorides may be bound to the type 2 copper

Topics: Caltech Library Services
Publisher: 'Proceedings of the National Academy of Sciences'
Year: 1978
OAI identifier: oai:authors.library.caltech.edu:1118

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