13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of heme proteins.
13CN ion appears to have the greatest potential to probe the heme environment of the ferric heme proteins; however, a resonance of the iron-bound (13)CN ion in ferric heme proteins has not yet been located. We show here the first detection of (13)C NMR signals of the iron-bound (13)CN for heme proteins and their model complexes in an unexpectedly large upfield region. This study demonstrates that the (13)C NMR signal of the iron-bound (13)CN is a sensitive probe to study the nature of the proximal ligand in ferric heme protein.
Fujii
Hiroshi
H
Institute for Molecular Science and Center for Integrative Bioscience, Okazaki National Research Institutes, Myodaiji, Okazaki 444-8585, Japan. hiro@ims.ac.jp
D000818:Animals; D002247:Carbon Isotopes; D003486:Cyanides / Q000737:chemistry* / Q000378:metabolism; D003574:Cytochrome c Group / Q000737:chemistry / Q000378:metabolism; D005290:Ferric Compounds / Q000737:chemistry* / Q000378:metabolism; D006420:Hemeproteins / Q000737:chemistry* / Q000378:metabolism; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000378:metabolism; D006736:Horses; D006801:Humans; D007093:Imidazoles / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011524:Protoporphyrins / Q000737:chemistry; D014907:Whales
D002247:Carbon Isotopes; D003486:Cyanides; D003574:Cytochrome c Group; D005290:Ferric Compounds; D006420:Hemeproteins; D006454:Hemoglobins; D007093:Imidazoles; D009211:Myoglobin; D011524:Protoporphyrins; D006735:Horseradish Peroxidase; C041104:dimethyl protoporphyrin IX