The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins

E.H Harutyunyan, I.P Kuranova, G.V Oblamova, A.N Popov, T.N Safonova, A.V Teplyakov, B.K Vainshtein, Julie C. Wilson, Guy Dodson

Research output: Contribution to journalArticlepeer-review

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 Angstrom 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. (C) 1996 Academic Press Limited

Original languageEnglish
Pages (from-to)152-161
Number of pages10
JournalJournal of Molecular Biology
Volume264
Issue number1
DOIs
Publication statusPublished - 22 Nov 1996

Keywords

  • leghaemoglobin
  • X-ray structure
  • carbon monoxide binding
  • nitric oxide binding
  • ligand geometry
  • SPERM WHALE MYOGLOBIN
  • X-RAY STRUCTURE
  • LIGAND-BINDING
  • RESONANCE RAMAN
  • INFRARED-SPECTROSCOPY
  • NEUTRON-DIFFRACTION
  • NITROSYL-ALPHA
  • HEME-PROTEINS
  • LEGHEMOGLOBIN
  • CO

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