Circular dichroism spectroscopy of Lucina I hemoglobin

FEBS Letters

Wittenberg, Jonathan B²  Chiancone, Emilia¹  Boffi, Alberto¹ 

[1] CNR Center of Molecular Biology c/o Department of Biochemical Sciences ‘A. Rossi Fanelli’, University La Sapienza, P. le Aldo Moro 5, 00185 Rome Italy;Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, NY USA

关键词: Hemoglobin;    Circular dichroism;    Heme Cotton effect;    Heme chirality;   

DOI  :  10.1016/S0014-5793(97)00727-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The monomeric hemoglobin from the mollusc Lucina pectinata (HbI) represents an interesting model system for the study of heme-related circular dichroic (CD) bands in view of the highly asymmetric distribution of aromatic residues around the heme pocket revealed by the X-ray crystal structure. The CD spectra of both ferrous and ferric HbI derivatives exhibit negative CD bands in the Soret and ultraviolet region with an enhanced ellipticity of the heme N and L bands in the near-UV region. In contrast, the magnitude of the Cotton effect in the visible and Soret regions is comparable to that observed in other hemoproteins. The spectrum of the carbon monoxide derivative shows a surprising similarity with that observed for the soybean leghemoglobin carbon monoxide adduct. A common structural feature in the two proteins is the presence in the distal pocket of two Phe residues (B9 and B10) the aromatic rings of which are perpendicular to the heme plane.

【 授权许可】

Unknown