Sökning: WFRF:(Kübel Joachim 1988)
> (2023) >
Ground-state hetero...
-
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.
(författare)
Ground-state heterogeneity and vibrational energy redistribution in bacterial phytochrome observed with femtosecond 2D IR spectroscopy
- Artikel/kapitelEngelska2023
Förlag, utgivningsår, omfång ...
Nummerbeteckningar
-
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
Kompletterande språkuppgifter
Ingår i deldatabas
Klassifikation
-
Ämneskategori:ref swepub-contenttype
-
Ämneskategori:art swepub-publicationtype
Anmärkningar
-
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.
Ämnesord och genrebeteckningar
Biuppslag (personer, institutioner, konferenser, titlar ...)
-
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
(författare)
-
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
(författare)
-
Salvadori, G.Univ Pisa, Dept Chem & Ind Chem, Via G Moruzzi 13, I-56126 Pisa, Italy.
(författare)
-
Mennucci, B.Univ Pisa, Dept Chem & Ind Chem, Via G Moruzzi 13, I-56126 Pisa, Italy.
(författare)
-
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
(författare)
-
Maj, MichalUppsala universitet,Fysikalisk kemi(Swepub:uu)micma447
(författare)
-
Göteborgs universitetInstitutionen för kemi och molekylärbiologi
(creator_code:org_t)
Sammanhörande titlar
-
Ingår i:Journal of Chemical Physics: AIP Publishing158:80021-96061089-7690
Internetlänk
Hitta via bibliotek
Till lärosätets databas