TY - JOUR
T1 - Control of the active site structure of giant bilayer hemoglobin from the Annelid Eisenia foetida using hierarchic assemblies
AU - Girasole, Marco
AU - Arcovito, Alessandro
AU - Marconi, Augusta
AU - Davoli, Camilla
AU - Congiu Castellano, Agostina
AU - Bellelli, Andrea
AU - Amiconi, Gino
PY - 2005
Y1 - 2005
N2 - The active site structure of the oxygenated derivative of the main subassemblies (whole protein, dodecamers, and trimers) of the giant haemoglobin from Eisenia foetida has been characterized by x-ray absorption near edge structure spectroscopy. The data revealed a remarkable effect of the hierarchic assemblies on the active site of the subunit. Specifically, the whole protein has the same site structure of the dodecamer, while a sharp conformational transition occurs when the dodecamer is disassembled into trimers (and monomers) revealing that constraints due to the protein matrix determine the active site geometry and, consequently, the protein function in these large complexes.
AB - The active site structure of the oxygenated derivative of the main subassemblies (whole protein, dodecamers, and trimers) of the giant haemoglobin from Eisenia foetida has been characterized by x-ray absorption near edge structure spectroscopy. The data revealed a remarkable effect of the hierarchic assemblies on the active site of the subunit. Specifically, the whole protein has the same site structure of the dodecamer, while a sharp conformational transition occurs when the dodecamer is disassembled into trimers (and monomers) revealing that constraints due to the protein matrix determine the active site geometry and, consequently, the protein function in these large complexes.
KW - XANES
KW - giant hemoglobin
KW - XANES
KW - giant hemoglobin
UR - http://hdl.handle.net/10807/6805
M3 - Article
SN - 0003-6951
SP - 4924
EP - 4929
JO - Applied Physics Letters
JF - Applied Physics Letters
ER -