Abstract

The major goal of time-resolved absorption and Raman spectroscopy on photodissociated ligand hemoglobin has been to provide a detailed description of the events occurring after dissociation of the ligand and to relate these events to the mechanism through which the protein controls the iron—ligand dissociation and binding properties. We report transient absorption spectra in the Soret band and Raman spectra measured at room temperature for human hemoglobin, myoglobin, and α or β subunits in the femtosecond and picosecond domain following photodissociation of the CO, O₂, or NO ligand complex with 120 fs or picosecond laser pulses.

© 1986 Optical Society of America