Revealing Ultrafast Two-Electron Transfer Over Tryptophan with Mass Spectrometry

18 June 2020, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Electron transfer crucial to bioenergetics is ubiquitously present in biological systems but most of them escape from direct observations. By using tryptophan and its derivatives with 1-CH3, 2-CH3, 5-CH3 and 5-OH substitutions as model molecules, we have unambiguously demonstrated successive two-electron transfer to tryptophan as well as electronic and vibrational excited molecular dissociation with mass spectrometry. The ultra-short time delay between two electrons down to sub-attosecond over a distance less than 10 Å was found to cause the strong coupling of electronic and vibrational excitations that was validated by the observation of radical-radical coupling. Intramolecular H migrations along with two-electron transfer was demonstrated with H/D exchange and 13C stable isotope labeling. This proposed technique allows us to observe the ultrafast electron transfer from tryptophan to the heme group in myoglobin proteins. It bridges electron transfer to energy transfer that has been revealed in FRET alone. FeII (porph•‐) and FeI (porph•‐) resulting from one- and two-electron transfer, respectively, have been unambiguously identified


Electron transfer
H migration
H/D exchange
Mass spectrometry
Stable isotope labeling

Supplementary materials

Supporting Information-Zhong-revised


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