期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 1, 期 19, 页码 2793-2799出版社
AMER CHEMICAL SOC
DOI: 10.1021/jz101049v
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资金
- Human Frontiers Science Program Organization [CDA0016/2007-C]
- NIH [GM063805]
- OCAST [HR07-1355]
- Oklahoma State University
The ultrafast excited-state dynamics underlying the receptor state photorecovery is resolved in the M100A mutant of the photoactive yellow protein (PYP) from Halorhodospira halophila. The M100A PYP mutant, with its distinctly slower photocycle than wt PYP, allows isolation of the pB signaling state for study of the photodynamics of the protonated chromophore cis-p-coumaric acid. Transient absorption signals indicate a subpicosecond excited-state proton-transfer reaction in the pB state that results in chromophore deprotonation prior to the cis-trans isomerization required in the photorecovery dynamics of the pG state. Two terminal photoproducts are observed, a blue-absorbing species presumed to be deprotonated trans-p-coumaric acid and an ultraviolet-ansorbing protonated photoproduct. These two photoproducts are hypothesized to originated from an equilibrium of open and closed folded forms of the signaling state, I-2 and I-2'.
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