Abstract
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.
Original language | English |
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Pages (from-to) | 1612-1622 |
Number of pages | 11 |
Journal | Biophysical Journal |
Volume | 66 |
Issue number | 5 |
DOIs | |
State | Published - 1994 |