A Steric Mechanism for Inhibition of CO Binding to Heme Proteins

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Science  16 Apr 1999:
Vol. 284, Issue 5413, pp. 473-476
DOI: 10.1126/science.284.5413.473

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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.

  • * Present address: European Molecular Biology Laboratory Outstation, Notkestraβe 85, 22603 Hamburg, Germany.

  • To whom correspondence should be addressed. E-mail: bartunik{at}

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