Control of the active site structure of giant bilayer hemoglobin from the Annelid Eisenia foetida using hierarchic assemblies (Articolo in rivista)

Type
Label
  • Control of the active site structure of giant bilayer hemoglobin from the Annelid Eisenia foetida using hierarchic assemblies (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Girasole M.1, Arcovito A.2, Marconi A.3, Davoli C.4, Congiu-Castellano A.5, Bellelli A.6, Amiconi G.7 (2005)
    Control of the active site structure of giant bilayer hemoglobin from the Annelid Eisenia foetida using hierarchic assemblies
    in Applied physics letters
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Girasole M.1, Arcovito A.2, Marconi A.3, Davoli C.4, Congiu-Castellano A.5, Bellelli A.6, Amiconi G.7 (literal)
Pagina inizio
  • 233901 (literal)
Pagina fine
  • 233901 (literal)
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  • Impact Factor = 4.127 (literal)
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  • 87 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
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  • 1 = Istituto di Struttura della Materia-CNR, 00133 Roma, Italy; 2 = Department of Biochemistry and Biophysics, Stockholm University, SE 10691 Stockholm, Sweden and Dipartimento Scienze Biochimiche, Università “La Sapienza,” 00185 Roma, Italy; 3,4 = Istituto di Neurobiologia e Medicina Molecolare-CNR, 00133 Roma, Italy; 5 = Dipartimento Fisica, Università “La Sapienza,” 00185 Roma, Italy; 6,7 = Dipartimento Scienze Biochimiche, Università “La Sapienza,” 00185 Roma, Italy. (literal)
Titolo
  • Control of the active site structure of giant bilayer hemoglobin from the Annelid Eisenia foetida using hierarchic assemblies (literal)
Abstract
  • 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. (literal)
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