Long-range electron-transfer in blue copper proteins

Creators: Gray, Harry B.

Abstract

It is widely recognized that blue copper proteins function as electron-transfer agents in biological systems.(1-10) Plastocyanin, for example, which is one of the most thoroughly studied of all the blue copper proteins, is a key component of the electron-transfer apparatus in the chloroplasts of green leaves. In its oxidized form, here referred to as the Cu2 + state, it is intensely blue, because of 600 nm absorption attributable to charge transfer from a cysteine sulphur to the copper. The review by Sykes,(9) based on his Tilden Lecture, is an excellent place to read about the structure and properties of plastocyanin.

Additional Information

© 1986 Royal Society of Chemistry. Delivered at a Symposium of the Dalton Division of the Royal Society of Chemistry, Scientific Societies' Lecture Theatre, London, on 14th March, 1985. I acknowledge with thanks the hospitality of the Department of Chemistry, University of California, Berkeley, where my Centenary Lecture manuscript was completed. Thanks also are due to my co-workers, especially N.M. Kostic, R. Margalit, C.-M. Che, D.F. Blair, H.-J. Chiang, I. Pecht, J.B. Shelton, J.R. Shelton, W.A. Schroeder, B.S. Brunschwig, P.J. DeLaive, A.M. English, M. Goldberg, S.L. Mayo, N. Sutin, B.G. Malmstrom, and W.R. Ellis, Jr., for their many contributions to the work I discussed in the lecture. Research on copper proteins at the California Institute of Technology is supported by National Institutes of Health Grant AM19038; this is Contribution No. 7313 from the Arthur Amos Noyes Laboratory.

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