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Science 16 April 1999:
Vol. 284. no. 5413, pp. 473 - 476
DOI: 10.1126/science.284.5413.473
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Reports

A Steric Mechanism for Inhibition of CO Binding to Heme Proteins

Galina S. Kachalova, Alexander N. Popov, * Hans D. Bartunik dagger

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.

Max-Planck-Arbeitsgruppen für Strukturelle Molekularbiologie, Arbeitsgruppe Proteindynamik, Notkestrabeta e 85, 22603 Hamburg, Germany.
*   Present address: European Molecular Biology Laboratory Outstation, Notkestrabeta e 85, 22603 Hamburg, Germany.

dagger    To whom correspondence should be addressed. E-mail: bartunik{at}mpghdb.desy.de

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