Abstract
The cycle of the photoactive yellow protein (PYP) has been extensively studied, but the dynamics of the isolated chromophore responsible for transduction is unknown. Here, we present real-time observation of the dynamics of the negatively charged chromophore and detection of intermediates along the path of trans-to-cis isomerization using femtosecond mass selection/electron detachment techniques. The results show that the role of the protein environment is not in the first step of double-bond twisting (barrier crossing) but in directing efficient conversion to the cis-structure and in impeding radical formation within the protein.
Original language | English |
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Pages (from-to) | 258-262 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 103 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2006 Jan 10 |
Externally published | Yes |
Keywords
- Femtobiology
- Molecular dynamics
- Photoelectron spectroscopy
- Transduction
ASJC Scopus subject areas
- General