In Situ Study of the Function of Bacterioruberin in the Dual-Chromophore Photoreceptor Archaerhodopsin-4
| Autor: | Xin Zhao, Sijin Chen, Haolin Cui, Anthony Watts, Yanan Yang, Xiaoyan Ding, Chao Sun |
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| Rok vydání: | 2018 |
| Předmět: |
Halobacterium salinarum
0301 basic medicine Archaeal Proteins Kinetics 010402 general chemistry 01 natural sciences Catalysis 03 medical and health sciences chemistry.chemical_compound Adenosine Triphosphate Protein structure Isomerism Amino Acid Sequence Peptide sequence biology Protein Stability Chemistry Retinal General Medicine General Chemistry Chromophore biology.organism_classification Carotenoids 0104 chemical sciences 030104 developmental biology Biophysics Bacterial rhodopsins Protein Multimerization Sequence Alignment Adenosine triphosphate |
| Zdroj: | Angewandte Chemie International Edition. 57:8937-8941 |
| ISSN: | 1433-7851 |
| DOI: | 10.1002/anie.201803195 |
| Popis: | While certain archaeal ion pumps have been shown to contain two chromophores, retinal and the carotenoid bacterioruberin, the functions of bacterioruberin have not been well explored. To address this research gap, recombinant archaerhodopsin-4 (aR4), either with retinal only or with both retinal and bacterioruberin chromophores, was successfully expressed together with endogenous lipids in H. salinarum L33 and MPK409 respectively. In situ solid-state NMR, supported by molecular spectroscopy and functional assays, revealed for the first time that the retinal thermal equilibrium in the dark-adapted state is modulated by bacterioruberin binding through a cluster of aromatic residues on helix E. Bacterioruberin not only stabilizes the protein trimeric structure but also affects the photocycle kinetics and the ATP formation rate. These new insights may be generalized to other receptors and proteins in which metastable thermal equilibria and functions are perturbed by ligand binding. |
| Databáze: | OpenAIRE |
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