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Published June 1, 1977 | public
Book Section - Chapter

Structure and Electron Transfer Reactions of Blue Copper Proteins

Abstract

Complete assignments of the electronic spectra of stellacyanin, plastocyanin, and azurin have been made. Bands attributable to d-d transitions have been located in the near-infrared region for the first time, and their positions are consistent with a distorted tetrahedral geometry for the blue copper center. The kinetics of the electron transfer reactions of stellacyanin, azurin, and plastocyanin with Fe(EDTA)^(2-) and Co(phen)_3^(3+) have been studied. Kinetic parameters indicate that reduction of azurin and plastocyanin by Fe(EDTA)^(2-) occurs by long distance transfer to a buried blue copper center. However, the pathway for oxidation involves substantial protein rearrangement, thereby allowing contact of Co(phen)_3^(3+) with the copper ligands. In contrast, the blue copper center of stellacyanin is equally accessible in solution to redox agents.

Additional Information

© 1977 American Chemical Society. Received July 26, 1976. Published in print 1 June 1977. We thank F. C. Anson and F. J. Grunthaner for helpful discussions. Research on blue copper proteins at the California Institute of Technology has been supported by the National Science Foundation. This paper is contribution no. 5366 from the Arthur Amos Noyes Laboratory of Chemical Physics.

Additional details

Created:
August 19, 2023
Modified:
January 14, 2024