Open AccessBinding of Carbon Monoxide to α‐Hemocyanin and β‐Hemocyanin from Helix pomatia
Author(s) -
KUIPER Harry A.,
TORENSMA Ruurd,
BRUGGEN Ernst F. J.
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10829.x
Subject(s) - helix pomatia , hemocyanin , carbon monoxide , bohr effect , chemistry , snail , oxygen , biophysics , inorganic chemistry , biochemistry , biology , ecology , catalysis , organic chemistry , oxygen–haemoglobin dissociation curve , antigen , genetics
The binding of carbon monoxide to α and β‐hemocyanin from the snail Helix pomatia was studied under equilibrium conditions. Homotropic interactions upon carbon monoxide binding were much weaker than upon the binding of oxygen. Heterotropic interactions (Bohr effect and calcium‐ion effect), however, were just as strong as in the case of the binding of oxygen. For α‐hemocyanin a linkage has been observed between the binding of carbon monoxide and a change in quaternary structure of the protein