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  • Chenchiliyan, ManoopGothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,Univ Gothenburg, Dept Chem & Mol Biol, Box 462, S-40530 Gothenburg, Sweden. (author)

Ground-state heterogeneity and vibrational energy redistribution in bacterial phytochrome observed with femtosecond 2D IR spectroscopy

  • Article/chapterEnglish2023

Publisher, publication year, extent ...

  • AIP Publishing,2023

Numbers

  • LIBRIS-ID:oai:gup.ub.gu.se/324882
  • https://gup.ub.gu.se/publication/324882URI
  • https://doi.org/10.1063/5.0135268DOI
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-499160URI

Supplementary language notes

  • Language:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Phytochromes belong to a group of photoreceptor proteins containing a covalently bound biliverdin chromophore that inter-converts between two isomeric forms upon photoexcitation. The existence and stability of the photocycle products are largely determined by the protein sequence and the presence of conserved hydrogen-bonding interactions in the vicinity of the chromophore. The vibrational signatures of biliverdin, however, are often weak and obscured under more intense protein bands, limiting spectroscopic studies of its non-transient signals. In this study, we apply isotope-labeling techniques to isolate the vibrational bands from the protein-bound chromophore of the bacterial phytochrome from Deinococcus radiodurans. We elucidate the structure and ultrafast dynamics of the chromophore with 2D infra-red (IR) spectroscopy and molecular dynamics simulations. The carbonyl stretch vibrations of the pyrrole rings show the heterogeneous distribution of hydrogen-bonding structures, which exhibit distinct ultrafast relaxation dynamics. Moreover, we resolve a previously undetected 1678 cm(-1) band that is strongly coupled to the A- and D-ring of biliverdin and demonstrate the presence of complex vibrational redistribution pathways between the biliverdin modes with relaxation-assisted measurements of 2D IR cross peaks. In summary, we expect 2D IR spectroscopy to be useful in explaining how point mutations in the protein sequence affect the hydrogen-bonding structure around the chromophore and consequently its ability to photoisomerize to the light-activated states.

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  • Kübel, Joachim,1988Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,Univ Gothenburg, Dept Chem & Mol Biol, Box 462, S-40530 Gothenburg, Sweden.(Swepub:gu)xkubjo (author)
  • Ooi, Saik AnnGothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,Univ Gothenburg, Dept Chem & Mol Biol, Box 462, S-40530 Gothenburg, Sweden.(Swepub:gu)xooisa (author)
  • Salvadori, G.Univ Pisa, Dept Chem & Ind Chem, Via G Moruzzi 13, I-56126 Pisa, Italy. (author)
  • Mennucci, B.Univ Pisa, Dept Chem & Ind Chem, Via G Moruzzi 13, I-56126 Pisa, Italy. (author)
  • Westenhoff, Sebastian,1978Uppsala universitet,Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,Biokemi,Univ Gothenburg, Dept Chem & Mol Biol, Box 462, S-40530 Gothenburg, Sweden.(Swepub:uu)sebwe861 (author)
  • Maj, MichalUppsala universitet,Fysikalisk kemi(Swepub:uu)micma447 (author)
  • Göteborgs universitetInstitutionen för kemi och molekylärbiologi (creator_code:org_t)

Related titles

  • In:Journal of Chemical Physics: AIP Publishing158:80021-96061089-7690

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