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Constraints of T conformation of carp azide hemoglobin on Fe site structure
Author(s) -
Bianconi A.,
Congiu-Castellano A.,
Dell'Ariccia M.,
Giovannelli A.,
Morante S.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80016-8
Subject(s) - xanes , wiggler , azide , chemistry , crystallography , ferric , porphyrin , synchrotron radiation , spectral line , absorption spectroscopy , photochemistry , inorganic chemistry , physics , organic chemistry , quantum mechanics , astronomy , cathode ray , electron
The iron site structure modifications induced by the transition from the quaternary R to T structure in ferric carp azide hemoglobin have been detected from analysis of multiple scattering resonances in the XANES (X‐ray absorption near edge structure) spectra. High signal‐to‐noise XANES spectra measured at the Frascati ‘wiggler’ synchrotron radiation facility reveal that the forces on the Fe active site, due to the transition from the R to T quaternary conformation, only induce the tilting of the porphyrin plane and probably also of the proximal histidine. The variation of the Fe‐N mean distance is not detected by XANES spectroscopy and therefore it is less than 0.01 Å.