Ultrafast electronic and vibrational dynamics of stabilized A state mutants of the green fluorescent protein (GFP): Snipping the proton wire |
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| Authors: | Deborah Stoner-Ma Andrew A Jaye Kate L Ronayne Jrme Nappa Peter J Tonge Stephen R Meech |
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| Institution: | aDepartment of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, USA;bCentral Laser Facility, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot, Oxon OX11 0QX, UK;cSchool of Chemical Sciences and Pharmacy, University of East Anglia, Norwich NR4 7TJ, UK |
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| Abstract: | Two blue absorbing and emitting mutants (S65G/T203V/E222Q and S65T at pH 5.5) of the green fluorescent protein (GFP) have been investigated through ultrafast time resolved infra-red (TRIR) and fluorescence spectroscopy. In these mutants, in which the excited state proton transfer reaction observed in wild-type GFP has been blocked, the photophysics are dominated by the neutral A state. It was found that the A* excited state lifetime is short, indicating that it is relatively less stabilised in the protein matrix than the anionic form. However, the lifetime of the A state can be increased through modifications to the protein structure. The TRIR spectra show that a large shifts in protein vibrational modes on excitation of the A state occurs in both these GFP mutants. This is ascribed to a change in H-bonding interactions between the protein matrix and the excited state. |
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| Keywords: | Ultrafast Transient infra-red Green fluorescent protein Proton transfer Fluorescence Protein dynamics Fluorescent protein |
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