Reports

Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O

Science  18 Aug 1995:
Vol. 269, Issue 5226, pp. 962-966
DOI: 10.1126/science.7638619

Abstract

The relative orientations of carbon monoxide (CO) bound toand photodissociated from myoglobin in solution have been determinedwith time-resolved infrared polarization spectroscopy. The bound CO isoriented < or = 7 degrees from the heme normal, corresponding tonearly linear FE-C-O. Upon dissociation from the Fe, CO becomestrapped in a docking site that orientationally constrains it to lieapproximately in the plane of the heme. Because the bound and "docked"CO are oriented in nearly orthogonal directions CO binding from thedocking site is suppressed. These solutions results help to establishhow myoglobin discriminates against CO, a controversial issuedominated by the misconception that Fe-C-O is bent.

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