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Haemocyanins

Published online by Cambridge University Press:  17 March 2009

K. E. van Holde  and
Karen I. Miller
K. E. van Holde
Affiliation:
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331
Karen I. Miller
Affiliation:
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331
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Extract

About ten years ago, one of the authors participated in a review of haemocyanin structure and function (van Holde & van Bruggen, 1971). At that time, it was possible to describe the field in terms of a limited amount of exciting new structural information, and a long list of unanswered questions. While the stoichiometry of oxygen binding was understood, virtually nothing was known about the active site. Even the oxidation state of the copper was a matter of conjecture. The size of the haemocyanin polypeptide chains was the subject of intense debate, with very little substantive knowledge available. While the haemocyanins were known to be allosteric proteins, there were virtually no experimental studies of oxygen binding on a level that could be meaningfully interpreted in terms of extant theories.

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Research Article
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Quarterly Reviews of Biophysics , Volume 15 , Issue 1 , February 1982 , pp. 1 - 129
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Copyright © Cambridge University Press 1982

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