Constraints of T conformation of carp azide hemoglobin on Fe site structure

FEBS Letters

Bianconi, A.¹  Congiu-Castellano, A.¹  Dell'Ariccia, M.¹  Giovannelli, A.¹  Morante, S.² 

[1] Dipartimento di Fisica, Universita La Sapienza, 00185 RomaItaly;Dipartimento di Fisica, Universita di Roma II, 00173 Roma, Italy

关键词: Hemoglobin;    Synchroton radiation;    XANES;   

DOI  :  10.1016/0014-5793(85)80016-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown