The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobin.
Heme proteins react inhomogeneously with ligands at cryogenic temperatures and homogeneously at room temperature. We have identified and characterized a transition from inhomogeneous to homogeneous behavior at intermediate temperatures in the time dependence of CO binding to horse myoglobin. The turnover is attributed to a functionally important tertiary protein relaxation process during which the barrier increases dynamically. This is verified by a combination of theory and multipulse measurements. A likely biological significance of this effect is in the autocatalysis of the ligand release process.
Agmon
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Department of Physical Chemistry, Hebrew University, Jerusalem, Israel.
Doster
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D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002248:Carbon Monoxide / Q000378:metabolism*; D002384:Catalysis; D006736:Horses; D066298:In Vitro Techniques; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics
D008024:Ligands; D009211:Myoglobin; D002248:Carbon Monoxide