A Steric Mechanism for Inhibition of CO Binding to Heme Proteins

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Abstract

The crystal structures of myoglobin in the deoxy-and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.

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