Spectroscopic and ligand-binding properties of an oxygen-binding heme protein from Chromatium vinosum.
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.
Gaul
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DF
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock 79409.
Davidson
M W
MW
Palmer
G
G
Shaw
R W
RW
Knaff
D B
DB
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
D001386:Azides; D003486:Cyanides; D006420:Hemeproteins; D010100:Oxygen