Entrapment and characterization of functional allosteric conformers of hemocyanin in sol–gel matrices

Hemocyanins are giant oxygen transport proteins of molluscs and arthropods, which display high cooperativity and a complex pattern of conformations, generated by hierarchical allosteric interactions of their complex quaternary structure. A still unanswered question is the correlation between the functional properties of the postulated conformers and structural features that govern their oxygen binding, such as metal complex coordination. In this study we focus on the dodecameric hemocyanin of the crustacean Carcinus aestuarii, with the aim to obtain a functional and structural characterization of the individual conformational states giving rise to cooperativity, by entrapping hemocyanin int…