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  Photodynamics of blue-light-regulated phosphodiesterase BlrP1 protein from Klebsiella pneumoniae and its photoreceptor BLUF domain

Tyagi, A., Penzkofer, A., Griese, J., Schlichting, I., Kirienko, N. V., & Gomelsky, M. (2008). Photodynamics of blue-light-regulated phosphodiesterase BlrP1 protein from Klebsiella pneumoniae and its photoreceptor BLUF domain. Chemical Physics Letters, 354(1), 130-141. doi:10.1016/j.chemphys.2008.10.003.

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Tyagi, A., Author
Penzkofer, A., Author
Griese, Julia1, Author              
Schlichting, Ilme1, Author              
Kirienko, Natalia V., Author
Gomelsky, Mark1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: BLUF domain; Blue-light-regulated phosphodiesterase (BlrP1); Klebsiella pneumoniae; Blue-light receptor; FAD; Absorption spectroscopy; Fluorescence spectroscopy; Photo-cycle; Photo-induced electron transfer; Photo-reduction
 Abstract: The BlrP1 protein from the enteric bacterium Klebsiella pneumoniae consists of a BLUF and an EAL domain and may activate c-di-GMP phosphodiesterase by blue-light. The full-length protein, BlrP1, and its BLUF domain, BlrP1_BLUF, are characterized by optical absorption and emission spectroscopy. The cofactor FAD in its oxidized redox state (FADox) is brought from the dark-adapted receptor state to the 10-nm red-shifted putative signalling state by violet light exposure. The recovery to the receptor state occurs with a time constant of about 1 min. The quantum yield of signalling state formation is about 0.17 for BlrP1_BLUF and about 0.08 for BlrP1. The fluorescence efficiency of the FADox cofactor is small due to photo-induced reductive electron transfer. Prolonged light exposure converts FADox in the signalling state to the fully reduced hydroquinone form FADredH− and causes low-efficient chromophore release with subsequent photo-degradation. The photo-cycle and photo-reduction dynamics in the receptor state and in the signalling state are discussed.

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Language(s): eng - English
 Dates: 2008-06-212008-10-082008-10-112008-12-10
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.chemphys.2008.10.003
 Degree: -

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Title: Chemical Physics Letters
  Other : Chem. Phys. Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : North-Holland
Pages: - Volume / Issue: 354 (1) Sequence Number: - Start / End Page: 130 - 141 Identifier: ISSN: 0009-2614
CoNE: https://pure.mpg.de/cone/journals/resource/954925389241