Abstract
We probed the heme iron motion for several proteins by measuring the evolution of the iron-histidine Raman band intensity during nitric oxide (NO) rebinding. Whereas NO dissociation induces quasi-instantaneous iron motion and heme doming, the reverse primary movement of the iron towards the planar heme after NO binding is delayed and varies among proteins (7–30 ps).
© 2010 Optical Society of America
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