We present a simple experimental setup for performing two-dimensional (2D) electronic spectroscopy in the partially collinear pump-probe geometry. The setup uses a sequence of birefringent wedges to create and delay a pair of phase-locked, collinear pump pulses, with extremely high phase stability and reproducibility. Continuous delay scanning is possible without any active stabilization or position tracking, and allows to record rapidly and easily 2D spectra. The setup works over a broad spectral range from the ultraviolet to the near-IR, it is compatible with few-optical-cycle pulses and can be easily reconfigured to two-colour operation. A simple method for scattering suppression is also introduced. As a proof of principle, we present degenerate and two-color 2D spectra of the light-harvesting complex 1 of purple bacteria.

/pdf/two-dimensional-electronic-spectroscopy-with-birefringent-3zoip5ycfs.pdf

Two-dimensional electronic spectroscopy with birefringent wedges

Orange carotenoid protein (OCP) is a water-soluble photoactive protein responsible for a photoprotective mechanism of nonphotochemical quenching in cyanobacteria. Under blue-green illumination, OCP converts from the stable orange into the signaling red quenching form; however, the latter form could also be obtained by chemical activation with high concentrations of sodium thiocyanate (NaSCN) or point mutations. In this work, we show that a single replacement of tryptophan-288, normally involved in protein-chromophore interactions, by alanine, results in formation of a new protein form, hereinafter referred to as purple carotenoid protein (PCP). Comparison of resonance Raman spectra of the native photoactivated red form, chemically activated OCP, and PCP reveals that carotenoid conformation is sensitive to the structure of the C-domain, implicating that the chromophore retains some interactions with this part of the protein in the active red form. Combination of differential scanning fluorimetry and picosecond time-resolved fluorescence anisotropy measurements allowed us to compare the stability of different OCP forms and to estimate relative differences in protein rotation rates. These results were corroborated by hydrodynamic analysis of proteins by dynamic light scattering and analytical size-exclusion chromatography, indicating that the light-induced conversion of the protein is accompanied by a significant increase in its size. On the whole, our data support the idea that the red form of OCP is a molten globule-like protein in which, however, interactions between the carotenoid and the C-terminal domain are preserved.

A comparative study of three signaling forms of the orange carotenoid protein

Fluorescent Labeling Preserving OCP Photoactivity Reveals Its Reorganization during the Photocycle

https://www.cell.com/biophysj/pdfExtended/S0006-3495(15)00662-1

The Signaling State of Orange Carotenoid Protein

Broadband two-dimensional electronic spectroscopy is applied to investigate the photophysics of the photoactive orange carotenoid protein, which is involved in nonphotochemical quenching in cyanobacteria. Differences in dynamics between the light and dark forms arise from the different structure of the carotenoid in the protein pocket, with consequences for the biological role of the two forms.

/pdf/comparing-the-photophysics-of-the-two-forms-of-the-orange-3zqa60qxmq.pdf

Comparing the photophysics of the two forms of the Orange Carotenoid Protein using 2D electronic spectroscopy

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Comparing the photophysics of the two forms of the Orange Carotenoid Protein using 2D electronic spectroscopy