Control of the active site structure of giant bilayer hemoglobin from the Annelid Eisenia foetida using hierarchic assemblies

Alessandro Arcovito, Marco Girasole, Augusta Marconi, Camilla Davoli, Agostina Congiu Castellano, Andrea Bellelli, Gino Amiconi

Risultato della ricerca: Contributo in rivistaArticolo in rivistapeer review

2 Citazioni (Scopus)

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.
Lingua originaleEnglish
pagine (da-a)4924-4929
Numero di pagine6
RivistaApplied Physics Letters
Stato di pubblicazionePubblicato - 2005

Keywords

  • XANES
  • giant hemoglobin

Fingerprint Entra nei temi di ricerca di 'Control of the active site structure of giant bilayer hemoglobin from the Annelid Eisenia foetida using hierarchic assemblies'. Insieme formano una fingerprint unica.

Cita questo