Photoactive Yellow Protein,
            <i>the</i>
            Xanthopsin

Horst, Michael; Hendriks, Johnny; Vreede, Jocelyne; Yeremenko, Sergei; Hellingwerf, Klaas J.

doi:10.1002/352760510x.ch19

Handbook of Photosensory Receptors 2005

DOI: 10.1002/352760510x.ch19

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Photoactive Yellow Protein, the Xanthopsin

Michael Horst

Johnny Hendriks

Jocelyne Vreede

et al.

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2013

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Cited by 2 publications

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“…PYP, from phototrophic bacterium Halorhodospira halophila, is a small water-soluble photoreceptor protein. It has been an attractive model for studying protein structures and dynamics . PYP gained further attention as a structural prototype for the PAS (Per-ARNT-Sim) and LOV (light, oxygen, or voltage) domains of a large class of receptor proteins.…”

mentioning

confidence: 99%

Raman Optical Activity Probing Structural Deformations of the 4-Hydroxycinnamyl Chromophore in Photoactive Yellow Protein

Shingae

Kubota

Kumauchi

et al. 2013

J. Phys. Chem. Lett.

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Many biological cofactors, such as light-absorbing chromophores in photoreceptors, contain a π-electron system and are planar molecules. These cofactors are, however, usually nonplanar within a protein environment, and such structural distortions have been shown to be functionally important. Because the nonplanar structure makes the molecule chiral, Raman optical activity (ROA) provides a wealth of stereochemical information about the structural and conformational details of cofactors. The present study applied a near-infrared excited ROA to photoactive yellow protein, a blue light receptor. We successfully obtained the ROA spectra of the 4-hydroxycinnamyl chromophore embedded in a protein environment. Furthermore, calculations of the ROA spectra utilizing density functional theory provide detailed structural information, such as data on out-of-plane distortions of the chromophore. The structural information obtained from the ROA spectra includes the positions of hydrogen atoms, which are usually not detected in the crystal structures of biological samples.

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mentioning

confidence: 99%

Raman Optical Activity Probing Structural Deformations of the 4-Hydroxycinnamyl Chromophore in Photoactive Yellow Protein

Shingae

Kubota

Kumauchi

et al. 2013

J. Phys. Chem. Lett.

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“…In the case of BR, we have shown that the all-trans/13-cis isomerization of the retinal chromophore significantly affects the ROA spectra. On the other hand, PYP, from phototrophic bacterium Halorhodospira halophila, contains the p -coumaric acid ( p CA) chromophore, which is covalently linked to Cys69 through a thiolester bond. , PYP is a small water-soluble photoreceptor protein, and it has been an attractive model for studying protein structures and dynamics . PYP gained further attention as a structural prototype for the PAS (Per-ARNT-Sim) and LOV (light, oxygen, or voltage) domains of a large class of receptor proteins.…”

mentioning

confidence: 99%

Active Site Structure of Photoactive Yellow Protein with a Locked Chromophore Analogue Revealed by Near-Infrared Raman Optical Activity

Kubota

Shingae

Foster

et al. 2013

J. Phys. Chem. Lett.

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Many biological cofactors, such as light-absorbing chromophores in photoreceptors, are intrinsically planar molecules. A protein environment, however, causes structural distortions of the cofactor, and such structural changes can lead to a modulation of chemical properties of the cofactor to maximize its biological activity. Here, we investigate the active site structure of photoactive yellow protein (PYP), a blue light photoreceptor that contains a p-coumaric acid (pCA) chromophore, by a near-infrared excited Raman optical activity (ROA). Specifically, we measured the ROA spectra of PYP, whose chromophore is replaced with a locked pCA analogue. Furthermore, we show that a spectral analysis based on quantum mechanical/molecular mechanical (QM/MM) calculations of the whole protein molecule is useful to obtain structural information from the observed ROA spectra. The use of the near-infrared ROA combined with QM/MM calculations is a novel and generally applicable spectroscopic tool to study the chromophore distortions within a protein environment. SECTION: Biophysical Chemistry and Biomolecules

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Photoactive Yellow Protein, the Xanthopsin

Cited by 2 publications

References 68 publications

Raman Optical Activity Probing Structural Deformations of the 4-Hydroxycinnamyl Chromophore in Photoactive Yellow Protein

Raman Optical Activity Probing Structural Deformations of the 4-Hydroxycinnamyl Chromophore in Photoactive Yellow Protein

Active Site Structure of Photoactive Yellow Protein with a Locked Chromophore Analogue Revealed by Near-Infrared Raman Optical Activity

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