The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins.
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.
Harutyunyan
E H
EH
Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia.
Safonova
T N
TN
Kuranova
I P
IP
Popov
A N
AN
Teplyakov
A V
AV
Obmolova
G V
GV
Valnshtein
B K
BK
Dodson
G G
GG
Wilson
J C
JC
D001665:Binding Sites; D002248:Carbon Monoxide / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004563:Electrochemistry; D007887:Fabaceae / Q000378:metabolism; D006418:Heme / Q000737:chemistry; D007700:Kinetics; D007874:Leghemoglobin / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D009569:Nitric Oxide / Q000737:chemistry / Q000378:metabolism*; D010946:Plants, Medicinal; D011485:Protein Binding; D017433:Protein Structure, Secondary
D007874:Leghemoglobin; D008024:Ligands; D009569:Nitric Oxide; D006418:Heme; D002248:Carbon Monoxide