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Literature DB >> 22010969

Ultrasensitive measurements of microbial rhodopsin photocycles using photochromic FRET.

Halil Bayraktar¹, Alexander P Fields, Joel M Kralj, John L Spudich, Kenneth J Rothschild, Adam E Cohen.

Abstract

Microbial rhodopsins are an important class of light-activated transmembrane proteins whose function is typically studied on bulk samples. Herein, we apply photochromic fluorescence resonance energy transfer to investigate the dynamics of these proteins with sensitivity approaching the single-molecule limit. The brightness of a covalently linked organic fluorophore is modulated by changes in the absorption spectrum of the endogenous retinal chromophore that occur as the molecule undergoes a light-activated photocycle. We studied the photocycles of blue-absorbing proteorhodopsin and sensory rhodopsin II (SRII). Clusters of 2-3 molecules of SRII clearly showed a light-induced photocycle. Single molecules of SRII showed a photocycle upon signal averaging over several illumination cycles.

Entities: CellLine Chemical Disease Gene Mutation Species

Mesh：

Substances：
Rhodopsin

Year: 2011 PMID： 22010969 PMCID： PMC3253248 DOI： 10.1111/j.1751-1097.2011.01011.x

Source DB: PubMed Journal: Photochem Photobiol ISSN： 0031-8655 Impact factor: 3.421

36 in total

1. Characterization of the proton-transporting photocycle of pharaonis halorhodopsin.

Authors: A Kulcsár; G I Groma; J K Lanyi; G Váró
Journal: Biophys J Date: 2000-11 Impact factor: 4.033

2. Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II.

Authors: A A Wegener; I Chizhov; M Engelhard; H J Steinhoff
Journal: J Mol Biol Date: 2000-08-25 Impact factor: 5.469

3. Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: a time-resolved fluorescence depolarization study.

Authors: U Alexiev; I Rimke; T Pöhlmann
Journal: J Mol Biol Date: 2003-05-02 Impact factor: 5.469

Ultrasensitive measurements of microbial rhodopsin photocycles using photochromic FRET.

1. Characterization of the proton-transporting photocycle of pharaonis halorhodopsin.

2. Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II.

3. Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: a time-resolved fluorescence depolarization study.

4. Sensory rhodopsin II from the haloalkaliphilic natronobacterium pharaonis: light-activated proton transfer reactions.

5. Conformational changes detected in a sensory rhodopsin II-transducer complex.

6. High-field EPR studies of the structure and conformational changes of site-directed spin labeled bacteriorhodopsin.

7. Electrical spiking in Escherichia coli probed with a fluorescent voltage-indicating protein.

8. FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor.

Review 9. Retinylidene proteins: structures and functions from archaea to humans.

10. Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin.

Review 1. Live-cell imaging of cell signaling using genetically encoded fluorescent reporters.

2. Rational design of a colorimetric pH sensor from a soluble retinoic acid chaperone.

Review 3. The evolving capabilities of rhodopsin-based genetically encoded voltage indicators.

Review 4. The Growing and Glowing Toolbox of Fluorescent and Photoactive Proteins.

Review 5. Voltage Imaging: Pitfalls and Potential.

6. Structural Changes in an Anion Channelrhodopsin: Formation of the K and L Intermediates at 80 K.

7. Using total internal reflection fluorescence microscopy to visualize rhodopsin-containing cells.

Review 8. Genetically encoded indicators of neuronal activity.

Review 9. Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals.

Review 10. Fluorescence spectroscopy of rhodopsins: insights and approaches.