Photoinduced ionization of the chromophore inside photoactive yellow protein (PYP) was investigated by ultrafast spectroscopy in the visible and near infrared spectral regions. An absorption band that extended from around 550nm to 850nm was observed and ascribed to solvated electrons, ejected from the p-hydroxycinnamic acid anion chromophore upon absorption of two 400nm photons. Global kinetic analysis showed that the solvated electron absorption decayed in two stages: a shorter phase of around 10ps and a longer phase of more than 3ns. From a simulation based on a diffusion model we conclude that the diffusion rate of the electron is about 0.8Å2/ps in wild type PYP, and that the electron is ejected to a short distance of only several angstroms away from the chromophore. The chromophore-protein pocket appears to provide a water-similar local environment for the electron. As mutations at different places around the chromophore have different effects to the electron recombination dynamics, we suggest that solvated electrons could provide a new method to investigate the local dielectric environment inside PYP and thus help to understand the role of the protein in the photoisomerization process.