Sökning: WFRF:(Kübel Joachim 1988)
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Ground-state hetero...
Ground-state heterogeneity and vibrational energy redistribution in bacterial phytochrome observed with femtosecond 2D IR spectroscopy
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- Chenchiliyan, Manoop (författare)
- Gothenburg 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.
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- Kübel, Joachim, 1988 (författare)
- Gothenburg 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.
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- Ooi, Saik Ann (författare)
- Gothenburg 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.
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- Salvadori, G. (författare)
- Univ Pisa, Dept Chem & Ind Chem, Via G Moruzzi 13, I-56126 Pisa, Italy.
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- Mennucci, B. (författare)
- Univ Pisa, Dept Chem & Ind Chem, Via G Moruzzi 13, I-56126 Pisa, Italy.
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- Westenhoff, Sebastian, 1978 (författare)
- Uppsala 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.
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- Maj, Michal (författare)
- Uppsala universitet,Fysikalisk kemi
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(creator_code:org_t)
- AIP Publishing, 2023
- 2023
- Engelska.
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Ingår i: Journal of Chemical Physics. - : AIP Publishing. - 0021-9606 .- 1089-7690. ; 158:8
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Abstract
Ämnesord
Stäng
- 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
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
- NATURVETENSKAP -- Kemi -- Teoretisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)
Nyckelord
- induced proton release
- chromophore
- bacteriophytochrome
- photoconversion
- biliverdin
- accuracy
- cofactor
- domain
- ftir
- Chemistry
- Physics
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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