Time-resolved X-ray absorption spectroscopy of carbon monoxide-myoglobin recombination after laser photolysis

Results are presented for the first time-resolved x-ray absorption measurements with a time resolution of 300 microseconds on a dynamically evolving chemical system. By synchronizing a neodymium:yttrium-aluminum-garnet pulsed laser with the bursts of x-rays emitted from the Cornell High Energy Synchrotron Source, it was possible to monitor at room temperature the recombination of carbon monoxide with myoglobin after laser photolysis. Changes in the pre-edge structure and in the position of the iron edge of this protein were detected as a function of time.