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.