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Structural and Vibrational Characterization of the Chromophore Binding Site of Bacterial Phytochrome Agp1
Citation key ISI:000401262000010
Author Takiden, Aref and Velazquez-Escobar, Francisco and Dragelj, Jovan and Woelke, Anna Lena and Knapp, Ernst-Walter and Piwowarski, Patrick and Bart, Franz and Hildebrandt, Peter and Mroginski, Maria Andrea
Pages 713-723
Year 2017
ISSN 0031-8655
DOI 10.1111/php.12737
Address 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Volume 93
Number 3
Publisher WILEY
Abstract Agp1 is a prototypical bacterial phytochrome from Agrobacterium fabrum harboring a biliverdin cofactor which reversibly photoconverts between a red-light-absorbing (Pr) and a far-red-light-absorbing (Pfr) states. The reaction mechanism involves the isomerization of the bilin-chromophore followed by large structural changes of the protein matrix that are coupled to protonation dynamics at the chromophore binding site. Histidines His250 and His280 participate in this process. Although the three-dimensional structure of Agp1 has been solved at high resolution, the precise position of hydrogen atoms and protonation pattern in the chromophore binding pocket has not been investigated yet. Here, we present protonated structure models of Agp1 in the Pr state involving appropriately placed hydrogen atoms that were generated by hybrid quantum mechanics/molecular mechanics- and electrostatic calculations and validated against experimental structural- and spectroscopic data. Although the effect of histidine protonation on the vibrational spectra is weak, our results favor charge neutral H250 and H280 both protonated at N epsilon. However, a neutral H250 with a proton at N epsilon and a cationic H280 may also be possible. Furthermore, the present QM/MM calculations of IR and Raman spectra of Agp1 containing isotope-labeled BV provide a detailed vibrational assignment of the biliverdin modes in the fingerprint region.
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