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Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin

Nature Structural Biology volume 4, pages 209–214 (1997)Cite this article

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.

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  1. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, 02138, USA

    Manho Lim, Timothy A. Jackson & Philip A. Anfinrud

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Lim, M., Jackson, T. & Anfinrud, P. Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin. Nat Struct Mol Biol 4, 209–214 (1997). https://doi.org/10.1038/nsb0397-209

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