ArticleThe journal of physical chemistry. B2026
Ultrafast Dynamics of rsCherryRev in Comparison with mCherry Reflecting Its Reversive Switchability.
Article in The journal of physical chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors.
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Abstract
Ultrafast dynamics of a red fluorescence protein mCherry and its reversibly switchable mutant rsCherryRev was studied by using a 10 fs visible pulse laser and fastscan transient absorption spectroscopy system. This mutation of mCherry for rsCherryRev has caused ultrafast relaxation with lifetimes of ∼0.3 ps and ∼3 ps much faster than the lifetime of mCherry (∼0.5 ns). The ultrashort lifetimes of rsCherryRev are considered to reflect the initial structural change of the chromophore during photoisomerization. The ultrashort duration of 10 fs laser pulse also visualizes that the C═C stretching mode intensity increases at ∼0.7 ps delay, reflecting the timing of photoisomerization in rsCherryRev.
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