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Electron Transfer Reactions of Copper Proteins

Holwerda, Robert A. and Wherland, Scot and Gray, Harry B. (1976) Electron Transfer Reactions of Copper Proteins. Annual Review of Biophysics and Bioengineering, 5 . pp. 363-396. ISSN 0084-6589. doi:10.1146/

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Copper proteins are a widespread and diverse class, isolated from plant, animal, bacterial, and fungal sources (1, 1a). The proteins considered here are involved in oxidation-reduction reactions, either as oxidoreductases or as electron carriers; other functions of copper proteins include metal ion storage and oxygen transport.

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Gray, Harry B.0000-0002-7937-7876
Additional Information:© 1976 Annual Reviews. We thank J. K. Beattie, L. Bennett, W. Blumberg, J. Coleman, C. Coyle, D. M. Dooley, J. A. Fee, D. J. Fensom, A. Finazzi-Agro, H. C. Freeman, P. Guerrieri, J. W. Hare, H. A. O. Hill, J. V. McArdle, D. R. McMillin, B. G. Malmström, J. L. Markley, B. Mondovi, L. Morpurgo, I. Pecht, J. Peisach, R. C. Rosenberg, G. Rotilio, N. SailasuUi, H. J. Schugar, O. Siiman, T. G. Spiro, N. Sutin, E. I. Solomon, T. Vanngård, and G. Yoneda for communicating ideas and results to us in advance of publication. One of us (H.B.G.) owes a special debt to Charles R. Dawson, who first stimulated his interest in the structures and reactions of blue proteins. Research at Caltech in the area of kinetics and mechanisms of copper protein redox reactions has been supported by the National Science Foundation. Research at Texas Tech University has been supported by the Research Corporation. S. Wherland acknowledges an NSF Graduate Fellowship for 1973-1975. This is Contribution No.5244 from the Arthur Amos Noyes Laboratory.
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Caltech Arthur Amos Noyes Laboratory5244
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Official Citation:Electron Transfer Reactions of Copper Proteins R A Holwerda, S Wherland, and H B Gray Vol. 5: 363–396
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:33004
Deposited By: Ruth Sustaita
Deposited On:08 Aug 2012 15:46
Last Modified:09 Nov 2021 21:31

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