title: Spectroscopic and ligand-binding properties of an oxygen-binding heme protein from Chromatium vinosum.
abstract: Magnetic circular dichroism spectra were obtained for the oxidized and reduced forms of cyanide, azide and carbon monoxide complexes of an O2-binding hemeprotein isolated from the photosynthetic purple sulfur bacterium, Chronatium vinosum. Cyanide binding to the protein, which results in formation of a low-spin complex, was highly pH dependent with little complex formation observed at pH values near or below 7.
authors: Department of Chemistry and Biochemistry, Texas Tech University, Lubbock 79409.
authors: D F
authors: DF
authors: Gaul
authors: M W
authors: MW
authors: Davidson
authors: G
authors: G
authors: Palmer
authors: R W
authors: RW
authors: Shaw
authors: D B
authors: DB
authors: Knaff
mesh_terms: D001386:Azides / Q000378:metabolism*; D002844:Chromatium / Q000032:analysis*; D002942:Circular Dichroism; D003486:Cyanides / Q000378:metabolism*; D006420:Hemeproteins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D013053:Spectrophotometry
chemical_list: D001386:Azides; D003486:Cyanides; D006420:Hemeproteins; D010100:Oxygen