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Published September 1978 | Published
Journal Article Open

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

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.

Additional Information

© 1978 by the National Academy of Sciences. Contributed by Harry B. Gray, June 5, 1978. We thank Prof. Maria Linder (California State University at Fullerton) for gel electrophoretic analysis and enzyme assays of purified protein samples, Dr. Lewis Larsen for supplying us with Cohn Fraction IV, and Dr. Lars Ryden for helpful discussions about the protein purification. This research was supported by National Science Foundation Grant CHE77-11389. J.H.D. gratefully acknowledges support from National Institutes of Health Postdoctoral Fellowship 1 F32CA05748-01 for 1976-1978. D.M.D. acknowledges a National Institutes of Health Predoctoral Traineeship (1974-1978). This is contribution 5801 from the Arthur Amos Noyes Laboratory. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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August 22, 2023
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