1GDI

CRYSTAL STRUCTURE OF FERRIC COMPLEXES OF THE YELLOW LUPIN LEGHEMOGLOBIN WITH ISOQUINOLINE AT 1.8 ANGSTROMS RESOLUTION (RUSSIAN)

Summary for 1GDI

• Entry DOI: 10.2210/pdb1gdi/pdb
• Descriptor: LEGHEMOGLOBIN (CARBONMONOXY), PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (4 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Lupinus luteus (yellow lupine)
• Total number of polymer chains: 1
• Total formula weight: 17318.57

Authors

Harutyunyan, E.,Safonova, T.,Kuranova, I. (deposition date: 1994-09-14, release date: 1995-02-27, Last modification date: 2024-02-07)

Primary citation

Harutyunyan, E.H.,Safonova, T.N.,Kuranova, I.P.,Popov, A.N.,Teplyakov, A.V.,Obmolova, G.V.,Valnshtein, B.K.,Dodson, G.G.,Wilson, J.C.
The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins.
J.Mol.Biol., 264:152-161, 1996

PubMed Abstract: Haemoglobins have the ability to discriminate between oxygen and other diatomic molecules. To further understanding of this process the X-ray crystal structures of carbonmonoxy and nitrosyl-leghaemoglobin have been determined at 1.8 A resolution. The ligand geometry is discussed in detail and the controversial issue of bent versus linear carbon monoxide binding is addressed. The bond angle of 160 degrees for CO-leghaemoglobin is in conflict with recent spectroscopy results on myoglobin but is consistent with angles obtained for myoglobin X-ray crystal structures. In contrast to the numerous carbon monoxide studies, very little stereochemical information is available for the nitric oxide adduct of haemoglobin. This is provided by the X-ray structure of NO-leghaemoglobin, which conforms to expected geometry with an Fe-NO angle of 147 degrees and a lengthened iron-proximal histidine bond. Thus crystallographic evidence is given for the predicted weakening of this bond on the binding of nitric oxide.

PubMed: 8950274
DOI: 10.1006/jmbi.1996.0630

Experimental method

X-RAY DIFFRACTION (1.8 Å)