Abstract
The nature of ligand motion within proteins has been investigated by measuring femtosecond time-resolved infrared (IR) spectra of CO photodissociated from the haem of myoglobin. Upon dissociation, the CO rotates approximately 90°and becomes trapped within a ligand docking site located near the binding site. Two trajectories, distinguished spectroscopically and kinetically with time constants of 0.20±0.05 ps and 0.52±0.10 ps, lead to CO located within the docking site with opposite orientations. The protein reorganizes about the 'docked' CO with a time constant of 1.6±0.3 ps and quickly establishes an energetic barrier that inhibits the reverse rebinding process.
Original language | English (US) |
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Pages (from-to) | 209-214 |
Number of pages | 6 |
Journal | Nature Structural Biology |
Volume | 4 |
Issue number | 3 |
DOIs | |
State | Published - Mar 1997 |
Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics