Conformational states of the Rapana thomasiana hemocyanin and its substructures studied by dynamic light scattering and time-resolved fluorescence spectroscopy.
Biophys J
; 88(2): 1276-82, 2005 Feb.
Article
em En
| MEDLINE
| ID: mdl-15533921
ABSTRACT
Hemocyanins are dioxygen-transporting proteins freely dissolved in the hemolymph of mollusks and arthropods. Dynamic light scattering and time-resolved fluorescence measurements show that the oxygenated and apo-forms of the Rapana thomasiana hemocyanin, its structural subunits RtH1 and RtH2, and those of the functional unit RtH2e, exist in different conformations. The oxygenated respiratory proteins are less compact and more asymmetric than the respective apo-forms. Different conformational states were also observed for the R. thomasiana hemocyanin in the absence and presence of an allosteric regulator. The results are in agreement with a molecular mechanism for cooperative dioxygen binding in molluscan hemocyanins including transfer of conformational changes from one functional unit to another.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Refratometria
/
Espectrometria de Fluorescência
/
Hemocianinas
/
Modelos Moleculares
/
Modelos Químicos
/
Moluscos
Limite:
Animals
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article