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Issue 9, 2015
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Influence of a chromophore analogue in the protein cage of a photoactive yellow protein

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Abstract

Time-resolved spectra of a photoactive yellow protein (PYP) containing cyano-p-coumaric acid (CHCA) were recorded. To understand the mechanism of photo-isomerization, an electron-withdrawing CN group was introduced into the PYP to alter the C[double bond, length as m-dash]C double bond character. Free CHCA chromophores in aqueous solution underwent photo-isomerization whereas PYP with a bound CHCA (PYP-CN) exhibited no photocycle at acidic or alkaline pH or in urea and other solutions. Furthermore, no photocycle was observed with PYP mutants after illumination. This phenomenon cannot be fully explained by the electron-withdrawing properties of the CN group. We conclude that the CHCA chromophore in PYP was locked in the protein cage and that the CN group interacted with the protein residues.

Graphical abstract: Influence of a chromophore analogue in the protein cage of a photoactive yellow protein

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Article information


Submitted
25 Apr 2015
Accepted
02 Jul 2015
First published
03 Jul 2015

Photochem. Photobiol. Sci., 2015,14, 1722-1728
Article type
Paper
Author version available

Influence of a chromophore analogue in the protein cage of a photoactive yellow protein

N. Hamada, Z. Tan, Y. Kanematsu, N. Inazumi and R. Nakamura, Photochem. Photobiol. Sci., 2015, 14, 1722
DOI: 10.1039/C5PP00176E

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