We report the first visible spectrum of a heme-protein in the gas phase. The aim of this work was to provide a reference for the optical absorption of an isolated heme-protein to better understand the influence of protein conformation and fluctuation and of solvent on its optical properties. After laser irradiation of gas-phase cytochrome c (cyt c), electron emission is observed. Electron photodetachment yield of cyt c 6- was recorded in the region of the Soret band of the porphyrin group, showing a maximum at 410 nm. Our results are compared with optical spectra of gas-phase heme and of cyt c in solution. We discuss the influence of the polypeptide chain and of the solvent on both the position and the broadening of the Soret band. Action spectrum of gas-phase cyt c is close to the absorption of native cyt c in solution, suggesting an efficient protection of the heme group from solvent accessibility by the polypeptide chain and similar interactions between the two moieties in solution and the gas phase.
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