How the CO in myoglobin acquired its bend: lessons in interpretation of crystallographic data.
Contrary to the expectation of chemists, the first X-ray structures of carbon monoxide bound to myoglobin (Mb) showed a highly distorted Fe-C-O bond system. These results appeared to support the idea of a largely steric mechanism for discrimination by the protein against CO binding, a lethal act for the protein in terms of its physiological function. The most recent independently determined high-resolution structures of Mb-CO have allowed the 25 year old controversy concerning the mode of CO binding to be resolved. The CO is now seen to bind in a roughly linear fashion without substantial bending, consistent with chemical expectations and spectroscopic measurements. Access to deposited diffraction data prompted a reevaluation of the sources of the original misinterpretation. A series of careful refinements of models against the data at high (1.1 A) and modest resolutions (1.5 A) have been performed in anisotropic versus isotropic modes. The results suggest that the original artifact was a result of lower quality crystals combined with anisotropic motion and limited resolution of the diffraction data sets. This retrospective analysis should serve as a caution for all researchers using structural tools to draw far-reaching biochemical conclusions.
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Department of Biochemistry and Cell Biology, W. M. Keck Center for Computational Biology, Rice University, Houston, TX 77005, USA.
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D002248:Carbon Monoxide / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation
D009211:Myoglobin; D002248:Carbon Monoxide