Haemocyanins

Author:

Holde K. E. van,Miller Karen I.

Abstract

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.

Publisher

Cambridge University Press (CUP)

Subject

Biophysics

Reference276 articles.

1. Bohr effect of the hemocyanin of the pearly nautilus, Nautilus macromphalus;Redmond;Spec. Sci. Tech.,1978

2. The respiratory proteins of the blood. II. The copper-combining ratio of oxygen and copper in some bloods containing hemocyanin;Redfield;J. biol. Chem.,1928

3. Presence of haemocyanin in the blood of a centipede Scutigera longicornis (Chilopoda: Myriapoda);Rajulu;Curr. Sci.,1969

4. Enzyme-metal-substrate complexes as coordination compounds;Orgel;Biochem. Soc. Symp.,1958

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