Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallography.

Abstract

We have developed the method of picosecond Laue crystallography and used this capability to probe ligand dynamics in tetrameric R-state hemoglobin (Hb). Time-resolved, 2 Å-resolution electron density maps of photolyzed HbCO reveal the time-dependent population of CO in the binding (A) and primary docking (B) sites of both α and β subunits from 100 ps to 10… (More)

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Cite this paper

@article{Schotte2013RealtimeTO, title={Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallography.}, author={Friedrich Schotte and Hyun Sun Cho and Jayashree Soman and Michael Wulff and John S Olson and Philip A. Anfinrud}, journal={Chemical physics}, year={2013}, volume={422}, pages={98-106} }