Nuclear-magnetic-resonance investigations of the biliverdin-apomyoglobin complex.

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  • Author(s): Marko H;Marko H; Müller N; Falk H
  • Source:
    European journal of biochemistry [Eur J Biochem] 1990 Oct 24; Vol. 193 (2), pp. 573-80.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
      Original Publication: Berlin, New York, Springer.
    • Subject Terms:
      Magnetic Resonance Spectroscopy*; Apoproteins/*chemistry ; Biliverdine/*chemistry ; Myoglobin/*chemistry; Animals ; Molecular Structure ; Whales
    • Abstract:
      The recently described biliverdin-apomyoglobin complex has been investigated by two-dimensional NMR methods and molecular modeling with respect to the geometry of the chromophore and its position within the myoglobin pocket. Nuclear Overhauser effect correlations between the ligand and apoprotein amino acid residues prove that the bile pigment assumes a cyclic helical conformation and a position similar to heme in native myoglobin.
    • Accession Number:
      0 (Apoproteins)
      0 (Myoglobin)
      0 (biliverdin-apomyoglobin complex)
      O9MIA842K9 (Biliverdine)
    • Publication Date:
      Date Created: 19901024 Date Completed: 19901213 Latest Revision: 20190620
    • Publication Date:
      20221208
    • Accession Number:
      10.1111/j.1432-1033.1990.tb19374.x
    • Accession Number:
      2226471