A Steric Mechanism for Inhibition of CO Binding to Heme Proteins
- 16 April 1999
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 284 (5413) , 473-476
- https://doi.org/10.1126/science.284.5413.473
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.Keywords
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