2007
DOI: 10.1021/ja074074n
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Ultrafast Structural Dynamics in BLUF Domains:  Transient Infrared Spectroscopy of AppA and Its Mutants

Abstract: The structural dynamics following photoexcitation of a photosensing BLUF (blue light sensing using FAD) domain protein have been investigated by ultrafast transient infrared spectroscopy. Specifically, the transcriptional antirepressor AppA from Rhodobacter sphaeroides has been studied in the light and dark adapted forms and in photoactive and inactive mutants W104F and Q63L. A transient absorption has been observed at 1666 cm(-1) which is a marker mode for the photoactive state of the protein. This instantane… Show more

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Cited by 115 publications
(207 citation statements)
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“…In BlrP1, these changes are accompanied by movement of a nearby methionine on the β5-strand of the BLUF domain, and both "Met in " and "Met out " arrangements have been described (15). The arrangement of Tyr-6, Gln-48, and Met-92 in the two forms of OaPAC is similar to that of the equivalent residues in BlrP1 ( visible FMN absorption bands to longer wavelength, and the carbonyl oxygen at C4 becomes a stronger hydrogen bond acceptor (16). The maximum absorption difference (light state minus dark state) in OaPAC is seen at a wavelength of 492 nm (Fig.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…In BlrP1, these changes are accompanied by movement of a nearby methionine on the β5-strand of the BLUF domain, and both "Met in " and "Met out " arrangements have been described (15). The arrangement of Tyr-6, Gln-48, and Met-92 in the two forms of OaPAC is similar to that of the equivalent residues in BlrP1 ( visible FMN absorption bands to longer wavelength, and the carbonyl oxygen at C4 becomes a stronger hydrogen bond acceptor (16). The maximum absorption difference (light state minus dark state) in OaPAC is seen at a wavelength of 492 nm (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…These vibrational responses to stimulation allow rapid signal transduction through a protein structure with minimal structural change. In fact, BLUF domains are known to photoactivate on a subnanosecond time-scale, faster than protein structural reorganization (16).…”
Section: Resultsmentioning
confidence: 99%
“…The TRIR spectra of dark-(dAppA BLUF ) and light-adapted (lAppA BLUF ) AppA BLUF contain a wealth of information on the early structural changes that accompany protein photoexcitation (11). However, in order to fully interpret the TRIR spectra and thereby enhance our understanding of the mechanism of AppA photoactivation, isotope labels must be incorporated site specifically into both the chromophore and the surrounding amino acids in order to assign vibrational modes associated with changes upon photoexcitation.…”
Section: Resultsmentioning
confidence: 99%
“…In various x-ray crystal and NMR solution structures (14)(15)(16)(17)(18)28), as well as spectroscopic (13,22,(39)(40)(41) and theoretical (42)(43)(44) studies, the dark-state orientation of Gln-63 has remained ambiguous. As illustrated in Fig.…”
Section: Structure Of the Bluf Domain Of Appamentioning
confidence: 99%