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

Publisher Website
Google Scholar
Abstract
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 I (blue) copper centers reversibly bleached are reported. The EPR spectrum of bleached [mammalian blood plasma] ceruloplasmin has a 7-line superhyperfine structure of the g.perp. region that is attributed to the presence of 3 N-donor type 2 Cu ligands. The EPR data suggest further that the type 2 Cu in ceruloplasmin possesses a tetragonal coordination gometry. In the presence of varying amounts of fluoride, superhyperfine splitting patterns in the g.dblvert. region of both ceruloplasmin derivatives indicate that a maximum of 2 fluorides may be bound to the type 2 Cu.