Abstract
Impulsive optical excitation has been performed on wild type, unligated leghemoglobin for the first time to compare the induced vibrational coherence with that observed in myoglobin. Both proteins were excited at the Soret maxima and probed at red and blue edges of the Soret band. The resulting kinetic traces were modulated by low-frequency vibrations. Leghemoglobin shows a decrease in vibrational amplitude compared with myoglobin. The possible cause for the amplitude differences is discussed in terms of contributions from both ground- and excited-state vibrational coherences and ground-state heterogeneity.
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