Abstract
Magnetic circular dichroism spectra were obtained for the oxidized and reduced forms of cyanide, azide and carbon monoxide complexes of an O 2-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.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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