Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
| Autor: | Francisco Velazquez Escobar, Yusaku Hontani, John T. M. Kennis, Daria M. Shcherbakova, Vladislav V. Verkhusha, Jörn Weißenborn, Mikhail Baloban, Miroslav Kloz, Maria Andrea Mroginski, Swetta A. Jansen |
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| Přispěvatelé: | Department of Anatomy, Medicum, Faculty of Medicine, University of Helsinki, Biophysics Photosynthesis/Energy, LaserLaB - Energy |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
MODEL COMPOUNDS 010402 general chemistry 01 natural sciences Biochemistry Molecular mechanics Article 03 medical and health sciences chemistry.chemical_compound PAS domain REVEALS polycyclic compounds Materials Chemistry Environmental Chemistry BACTERIOPHYTOCHROME OPTIMIZATION QD1-999 Cofactor binding SPECTROSCOPY Biliverdin CHROMOPHORE Hydrogen bond Tetrapyrrole binding PHOTOCHEMISTRY General Chemistry Tetrapyrrole STATE 0104 chemical sciences Chemistry INSIGHTS 030104 developmental biology INFRARED FLUORESCENT PROTEINS chemistry Covalent bond Biophysics 3111 Biomedicine |
| Zdroj: | Hontani, Y, Baloban, M, Escobar, F V, Jansen, S A, Shcherbakova, D M, Weißenborn, J, Kloz, M, Mroginski, M A, Verkhusha, V V & Kennis, J T M 2021, ' Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome ', Communications Chemistry, vol. 4, no. 1, 3, pp. 1-11 . https://doi.org/10.1038/s42004-020-00437-3 Communications chemistry Communications Chemistry, Vol 4, Iss 1, Pp 1-11 (2021) Communications Chemistry, 4(1):3, 1-11. Springer Nature |
| ISSN: | 2399-3669 |
| DOI: | 10.1038/s42004-020-00437-3 |
| Popis: | Near-infrared fluorescent proteins (NIR FPs) engineered from bacterial phytochromes are widely used for structural and functional deep-tissue imaging in vivo. To fluoresce, NIR FPs covalently bind a chromophore, such as biliverdin IXa tetrapyrrole. The efficiency of biliverdin binding directly affects the fluorescence properties, rendering understanding of its molecular mechanism of major importance. miRFP proteins constitute a family of bright monomeric NIR FPs that comprise a Per-ARNT-Sim (PAS) and cGMP-specific phosphodiesterases - Adenylyl cyclases - FhlA (GAF) domain. Here, we structurally analyze biliverdin binding to miRFPs in real time using time-resolved stimulated Raman spectroscopy and quantum mechanics/molecular mechanics (QM/MM) calculations. Biliverdin undergoes isomerization, localization to its binding pocket, and pyrrolenine nitrogen protonation in |
| Databáze: | OpenAIRE |
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