A steric mechanism for inhibition of CO binding to heme proteins |
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Authors: | Kachalova G S Popov A N Bartunik H D |
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Institution: | Max-Planck-Arbeitsgruppen für Strukturelle Molekularbiologie, Arbeitsgruppe Proteindynamik, Notkestrabetae 85, 22603 Hamburg, Germany. |
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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. |
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